BioQuakes

AP Biology class blog for discussing current research in Biology

Tag: science (Page 1 of 3)

Unlocking the Mysteries of the Brain: Bridging Neuroscience and AP Biology

In recent years, neuroscience has unveiled exciting breakthroughs in our understanding of the human brain, revealing its intricate nature. Thanks to the National Institutes of Health’s BRAIN Initiative and the work of the BRAIN Initiative Cell Census Network, we are now diving deeper into the cellular makeup of the brain. This research aligns with our AP Biology lessons on cell structure. It highlights the highly organized nature of nerve cells, reinforcing the concept that cells are the fundamental building blocks of life.

Neuron Cell Body

One remarkable achievement of this research is the creation of detailed cell maps of human and nonhuman primate brains. This development aligns with our AP Biology class, where we have learned about the fundamental concept of cell structure. Cells are, indeed, the building blocks of life, and this research demonstrates how, even in the complex nervous system, all cells exhibit a specific and organized arrangement.

This exploration also highlights the intriguing similarities in the cellular and molecular properties of human and nonhuman primate brains. These shared features reflect our evolutionary history and the conserved nature of brain structure across different species. The research suggests that slight changes in gene expression during human evolution have led to adaptations in neuronal wiring and synaptic function, contributing to our remarkable ability to adapt, learn, and change.

In our recent studies on neurons, we have learned about the fascinating world of these specialized cells. Our understanding of neuron structure and function provides a foundation for comprehending the significance of the research conducted under the BRAIN Initiative. This supports that the brain’s structure is not fixed but adapts to meet the challenges it faces.
The primary goal of the BRAIN Initiative Cell Census Network is to create a comprehensive record of brain cells. This understanding aids in comprehension of the development and progression of brain disorders. By learning the cellular composition of the brain, we can address the challenges that arise when things go wrong, promising a brighter future in the field of brain science.

As we reflect on these intriguing connections between neuroscience and our AP Biology knowledge, it is evident that our class has equipped us with a fundamental understanding of cell structure. This knowledge has proven invaluable in making sense of groundbreaking neuroscience research. I find this as a very intriguing and exciting journey, and scientists are actively committed to understanding the brain’s remarkable adaptability, the key to its functioning and evolution. As we explore the fascinating connections between neuroscience and our AP Biology knowledge, how could this deeper understanding of the brain’s adaptability and structure impact the future of healthcare and treatments for neurological conditions? Feel free to share your views and insights!

A New Approach to Wound Care

Researchers at Linköping University in Sweden have made an incredible contribution to the field of medicine, specifically in wound care and infection detection that does not interfere with the patient’s healing process.

In medicine, wounds are typically treated with a dressing, which is changed often to avoid infection. In order to detect infection, healthcare providers have to frequently open the wound’s covering, which can be painful and can potentially disrupt the healing process. Additionally, each time the wound is opened, the risk of infection is increased. The researchers were alarmed by this issue, and developed a wound dressing comprised of nanocellulose that has the ability to display early signs of infection without further tampering with the wound or lifting the dressing. Daniel Aili, a professor involved in the study, has confidently stated that “being able to see instantly whether a wound has become infected, without having to lift the dressing, opens up for a new type of wound care that can lead to more efficient care and improve life for patients with hard-to-heal wounds. It can also reduce unnecessary use of antibiotics.”

The new wound dressing is made of a tight mesh nanocellulose material, which prevents bacteria and other harmful microbes from entering the wound. However, the mesh-like material allows airflow in, which is critical in the wound healing process. However, if the wound does become infected, the nanocellulose dressing will display a shift in color, notifying healthcare providers that the wound needs care. pH also plays a major role in this creation. Wounds that are not infected maintain a pH value of about 5.5. If an infection occurs, the wound starts to become basic and can increase to a pH value of 8, or higher. The increase in pH occurs because the wound’s bacteria shift their pH to properly fit their optimal growth environment. As we learned in AP Biology class, bacteria and enzymes have an optimal pH level to grow and function. If this level is not maintained, they cannot function properly. So, the bacteria increase their pH in response to infection if the optimal level is compromised. This elevated pH level in the wound can be detected by the nanocellulose dressing before any physical signs of infection.

pH Value Scale

In order to make the nanocellulose display infection with an elevated pH value, the researchers used bromthymol blue, a dye that reacts to a change in pH value. The bromthymol blue shifts from yellow to blue if the pH value increases past 7. The material of the bromthymol was then able to be combined with the dressing material without ruining the nanocellulose. As a result, the researchers successfully developed a safe-to-use, noninvasive wound dressing that will display a blue color if an infection occurs.

Bromothymol blue colors at different pH levels

 

 Cancer Detection Using CRISPR Gene Editing

Currently, many are accustomed to invasive cancer diagnostic methods such as endoscopies, colonoscopies, and mammograms. Driven by the desire to discover new methods, a group of researchers from the American Cancer Society developed an alternative method, which is a significant contribution to cancer detection.

Utilizing CRISPR gene editing as their approach, the group of ACS researchers developed an easy-to-use mechanism for detecting small amounts of cancer in plasma. CRISPR gene editing is a method that scientists and researchers have been using to modify an organism’s DNA. CRISPR gene editing is often done for numerous reasons, such as adding or removing genetic material, creating immune defense systems, and repairing DNA. Their detection method also allows healthcare professionals in diagnostics to decipher between malignant and benign cancer-related molecules that they may discover.

CRISPR Gene-Editing

The first step that the researchers made to develop this approach was to design a CRISPR system that creates a manufactured exosome out of two reporter molecule fragments, which they cut. An exosome is a small vesicle that carries material such as lipids, proteins, and nucleic acids after branching out from a host cell. Exosomes are typically involved in detecting cancerous cells because they provide a glimpse into the host cell they branched out from. Therefore, cancerous cells are shown in their exosomes through biomarkers, like micro RNAs (miRNA). In AP Biology class, microRNAs are described as materials that bind to complementary mRNAs to prevent the translation from occurring. MiRNAs are a recent discovery, identified in 1993. It is now concluded that most gene expression is influenced by them, so the researchers made efficient use of miRNA in their experiment. The two fragments of the reporter molecule came together and interacted with the CRISPR’s materials.

Micro RNA Sequence

The researchers concluded that if the targeted miRNA sequence was evident in the combination, the CRISPR system they made would become activated and cut apart the reporter molecule. The researchers specifically targeted miRNA-21, which is often involved in cancer development. The researchers were able to detect miRNA within a combination of similar sequences and later tested their method on a group of healthy exosomes and cancerous exosomes. Their CRISPR system successfully differentiated between the healthy and cancerous exosomes, which makes this system effective for cancer detection. The researchers are confident that their CRISPR gene editing approach to cancer detection will make diagnosis easier on patients and a more efficient process overall.

 

A tree stump that should be dead, found alive!!!

A tree stump in New Zealand that should be dead, was found alive. Martin Bader and Sebastian Leuzinger, professors at the Auckland University of Technology discovered the tree stump during a hike in West Auckland. The stump didn’t have any foliage, which according to Merriam-Webster dictionary is
a cluster of leaves, flowers, and branches“. The two professors decided to investigate how the nearby trees were keeping the stump alive. It was found that the water flow to the tree stump “was strongly negatively correlated with that in the other trees”. It was then found that roots of the stump were grafted to the surrounding trees. These grafts, (“thick underground roots that are pressed together”) are solely what was keeping this stump alive. But now the question is why would the other trees want to keep this stump alive? There might be a possible explanations. Professor Leuzinger says that grafts were formed before the tree became a stump. Trees do this in order to access more nutrients from other trees. When this tree became a stump the grafts stay in tact. So when the other trees are receiving nutrients they are transferring to the stump unknowingly to keep it alive. This discovery could change the way scientists deal with survival of trees throughout climate change as well as the ecology of the forest.

AP BIO 

Trees constantly go through photosynthesis in order to survive. Photosynthesis in trees takes place inside the chloroplasts that are in the mesophyll of the tree. The leaves pull in carbon dioxide and water and use energy from the sun in order to feed the tree. The carbon dioxide and water are then converted into chemical compounds, like sugar, which fuels the trees life. Trees that have grafts then take the nutrients and transfer them to surrounding trees. The trees surrounding the tree stump took the nutrients gained from photosynthesis as well as nearby water to feed and keep the stump alive.

Adansonia digitata

Read it and wheat…

Wheat, corn, and rice are the most important crops around the world. As someone who enjoys baking, wheat is the base of almost all the desserts and bread recipes I bake. However, as I have become more interested in baking various types of bread, I wondered how gluten is formed and how bread textures change based on how long I kneaded the dough. According to Jessica R Biesiekierski in her article “What is Gluten”, Gluten is “complex mixture of hundreds of related but distinct proteins, mainly gliadin and glutenin.” The gluten matrix is essential to the quality of bread dough. It has the ability to act as a “binding” agent and is also used in marinades and even capsules in medication.  The biology of gluten and its structure depend on the ration of glutenin and gliadins. Each component has different functions that can effect “viscoelasticity”. In her article Biesiekiersk, worked to find evidence that “exposure to gluten may be increasing with changes in cereal technology”. There are many diets and intolerances caused by gluten such as the gluten free diet, gluten disorders, coeliac disease wheat allergy and sensitivity. In conclusion of their study, they determined “Gluten is a complex protein network and plays a key role in determining the rheological dough properties and baking qualities.” However, they came across a challenged. They learned that protein structure can “vary dependent on several factors”. Ultimately, make “analysis and definitions difficult”. And overall they conclude that “further work is needed to completely understand non-coeliac gluten sensitive”.

Another study that researched viscoelasticity is by is Peter R. Shewry, Nigel G. Halford, Peter S. Belton, and Arthur S. Tatham studied “The structure properties of gluten: an elastic protein from wheat grain”. According to Science Direct, viscoelasticity refers to a material’s tendency to act like a fluid or a solid. An additional article that explores viscoelasticity.

Vehnäpelto 6

They manipulate the “amount and composition” of HMM subunits concerning the strength or change of gluten structure and properties. These scholars describe wheat as a plant with many properties, however, they emphasized “viscoelasticity”. In terms of this research, viscoelasticity is “the balance between the extensibility and elasticity determining the end use quality.” The scholars use the dough as an example stating that “ highly elastic (‘strong’) doughs are required for bread making but, more extensible doughs are required for making cakes and biscuits”. In the study, these scholars focused on the HMM protein subunits of gluten. At least 50 different types of gluten proteins can be produced during the kneading process; however, these researchers have chosen to focus on the HMM subunits of glutenin. HMM, subunits, X type, and Y type can be only found on one chromosome in wheat cells. These two subunits are 70 % accountable for the viscoelastic variations in bread. This presentation allowed the researcher to see how stable and unstable the subunits were which would play a role in their ability to interact with peptides. In addition, these peptides may relate to the role of gluten in stabilizing the structures and interactions of the subunits.

US Navy 050102-N-5837R-011 Culinary Specialist 3rd Class Joshua Savoy and Culinary Specialist 3rd Class Davy Nugent prepares bread in the bakery aboard the Nimitz-class aircraft carrier USS Abraham Lincoln (CVN 72) Both articles emphasized the importance of protein structure. AP Biology greatly emphasizes the importance of Organic compounds. Proteins have a few structures that are ultimately composed of sequences of amino acids to create polypeptide chains. From primary structure proteins can become more complex by forming alpha helixes and beta pleated sheets. From that point 3D structures can be made. Gluten has a very structure characterized by “high allelic polymorphism encoding its specific proteins, glutenin, and gliadin”. This leads to wheat producing “unique types and quantities of these compounds”, these types and quantities can vary based off “growing conditions and technological processes”.

Self-Assembling Hydrophobic Sandwiches

You read that correctly! Researchers at Rice University in Houston, Texas alongside Jeffrey Hartgerink have made a significant advance in injury treatment, illness education, and drug candidate by testing the self-assembling abilities of 3D printed nanofibrous multidomain peptide hydrogels, referred to as “hydrophobic sandwiches.” 

Hydrogel

The main goal of Hartgerink’s team was to create a structure that could house cells and help them grow tissue by 3D printing the peptide ink. The printing allows researchers to recreate the complexity of biological structures due to their soft and flexible tissue-like feel, making this a major scientifical discovery and advantage. Hartgerink and his team describe their printed peptides as “hydrophobic sandwiches” due to their design, flexibility, and behavior. The peptides were printed to have one hydrophobic side and one hydrophilic side, allowing them to flip on top of each other when placed in water and resemble sandwiches. Like we learned in AP Biology, the hydrophillic qualities of one side will attract water, and the hydrophobic qualities of the other will repel water. Hydrophobic molecules repel water because they are nonpolar molecules, so they are not attracted to water, which is polar. Once the “sandwiches” were stacked after flipping in the water, they formed the hydrogels which can be vital to tissue engineering and wastewater treatments. 

Hydrogel Structure

The multidomain peptides have already been utilized due to their self-assembling nature for regenerating nerves, treating cancer, healing wounds, and encouraging tissue development throughout the body. Rather than only focusing on this aspect of the peptides, Adam Farsheed, a lead author in Hartgerink’s study, wanted to specifically highlight the fact that these peptides are an ideal 3D-printing ink choice due to their self-assembling nature. When testing the “sandwiches,” Farsheed took a unique, brute-force approach to add more of the material, rather than chemically modifying it, to test its function and ability to reassemble itself after deformation. He proved that adding more peptide material lets the peptide reassemble and heal itself extremely well after being deformed. This discovery will make the hydrogels an ideal candidate for scientific and medical usage.  

Through continued testing, he was also able to confirm that the peptides behave differently depending on their charge. The peptide cells with a negative charge tended to ball up on the substrate of the experiment and the positively charged cells spread out and started to mature on their own. Farsheed has confidently stated that their findings will allow the group to “control cell behavior using both structural and chemical complexity.” Both Hartgerink and Farsheed have made incredible contributions to the world of science through their studies using 3D-printed peptide hydrogels. 

 

A “Coffee-With-Milk” A Day Keeps The Doctor Away

In a recent study, researchers at the Department of Food Science, in collaboration with researchers from the Department of Veterinary and Animal Sciences, at the University of Copenhagen have discovered evidence that the mixture of coffee and milk has anti-inflammatory effects when consumed.

On January 30th, a study was published in the Journal of Agricultural and Food Chemistry (led by Professor Marianne Nissen Lund) that explains how this common combination of ingredients can limit inflammation.  To test the theory, the study “applied artificial inflammation to immune cells.  Some cells received various doses of polyphenols that had reacted with an amino acid, while others only received the same doses. A control group received nothing” (Science Daily).

The results showed that cells that received a dosage of polyphenols and amino acids were twice as effective as cells that received purely polyphenols.  Now, you may be asking how this relates to coffee and milk?  The answer to this question lies in the definitions of terms used above.  Polyphenols are a “category of plant compounds that offer health benefits” (Healthline).  They are found in coffee beans, and therefore, coffee.  Amino acids are “molecules that combine to form proteins,” and therefore are found in a majority of animal products, including milk (Medline Plus).

It is an established fact in the scientific community that polyphenols and amino acids bond, and therefore, the link between the two substances and anti-inflammatory effects is believable to scientists after the recent study performed by the Department of Food Science.  Furthermore, considering how common both substances are, it is likely that a similar reaction occurs when protein is combined with other fruits and vegetables with high amounts of polyphenol.  According to Marianne Nissen Lund, “I can imagine that something similar happens in, for example, a meat dish with vegetables or a smoothie, if you make sure to add some protein like milk or yogurt”.

The immune system is incredibly important to the function of the human body, as it serves to maintain order and defend against both foreign and local threats. When pathogens are able to infiltrate the body, they trigger innate immunity defenses, which in turn causes inflammation (as histamines which are released dilate local blood vessels and increase capillary permeability and cause the area to swell with fluid, which thus, causes inflammation).

Although immune cells (and in particular, innate immunity) cause inflammation, it is also the job of the immune system to limit inflammation by fighting off any unwanted antigen quickly, as the faster the antigen is killed, the faster inflammation goes away.  Immune cells of all types serve this function, ranging from innate to adaptive.  Thus, a compound that can increase the reaction rate of immune cells is incredibly valuable to animal health, including human health.

The results of the study show that polyphenols that have reacted with amino acids can double the effectiveness of the anti-inflammatory process of immune cells.  So, next time you are ordering a coffee, remember to ask for a splash of milk – you just might thank me later.

Coffee with milk (563800) (cropped)

Newly Discovered Neurons and Their Role in Maintaining Normal Body Temperature

The internal body temperature in humans and mammals is maintained at 37℃/96℉, unless disrupted by a force like an illness or heat exhaustion. Regulating the body to stay in the normal range is crucial for survival and for enzyme function.  Our internal body temperature is constantly being regulated by our hypothalamus, located at the base of our brain. The hypothalamus uses sensors from a mediator known as prostaglandin E which is brought about when an infection is present in the body. After PGE2 is present, it signals for the body to raise its temperature and combat the infection. If temperature levels are abnormal, the enzymes in our body have trouble functioning because they need specific temperature conditions to carry out reactions. Therefore, maintaining homeostasis throughout the body by regulating internal temperature is key to human survival.

Prostaglandin E

A team of researchers at Nagoya University in Japan were inspired by this process and decided to focus on the unknown neurons that make up the receptors of PGE2 and how this regulation process functions. The group of professors and colleagues successfully discovered key neurons that work to regulate the body temperature of mammals. This finding can be highly useful for creating future technology that can artificially fix body temperature related conditions such as hypothermia, heat stroke, and obesity.  

Neuron

Neuron

By using rats as a subject for their research, they exposed the rats to cold (4°C), room (24°C) and hot (36°C) temperatures to observe the effect of temperature changes on EP3 neuron response. After conducting the experiment, the researchers were able to conclude that exposure to the hot temperature led to an activation of EP3 neurons and the cold temperatures did not. Once they made this conclusion, they dug deeper into the neurons and analyzed the nerve fibers of the neurons to discover where the signal transmission occurs after sensing an infection. The researchers were able to conclude that the neuron fibers are spread out in different areas of the brain, mainly the dosomedial hypothalmus, which works to activate the sympathetic nervous system. Not only did they discover these fibers, but they also discovered the substance that EP3 neurons utilize to send signals to DMH. By observing the structure and chemical makeup, they found that this substance is a neurotransmitter known as gamma-aminobutyric acid (GABA), which inhibits neuron excitation. 

Finally, their findings support the idea that EP3 neurons are a major component of regulating internal body temperature and that they send out the GABA substance to signal to DMH neurons for a proper response. Their research proves that intiating a neural response decreases body temperature and inhibiting neurons leads to an increase in body temperature. Furthermore, their strong research in this area can support future development of advanced technology that will be capable of artificially adjusting internal body temperature. The anticipated technology could help prevent hypothermia, treat obesity to keep body temperature slightly higher and initiate fat burning, and be a key method of survival in hot environments. 

 

Ballerinas Got the Brains!

A 2013 research article conducted by scientists at the Imperial College of London has dived into the ballet world and researched the brains of ballerinas. Their research led to the discovery that dancers can suppress signals of dizziness using the balance organs of the inner ear. The vestibular system, found in the inner ear, consists mainly of smaller circular canals. Each canal recognizes different motions: Up and Down, Side to side, and tilting. These canals are filled with hair and liquid which move with your body to send signals to the brain using the acoustic nerve. With this information, your brain can process balance, dizziness, and vertigo. These researchers became curious about how ballet dancers can perform multiple balanced pirouettes without feelings of dizziness. And as a dancer, I would say this is because of the technique of spotting which involves rapidly moving the head to keep one’s eyes on a fixed spot.

However, this study has proved that wrong. So, with the help of 29 ballet dancers and 20 rowers, the researchers put it to the test. Their method of testing involved putting the volunteers in a dark room and spinning them on a rotating chair. They then timed how long it took for the dizziness to stop. In addition, the researchers measure eye reflexes triggered by the vestibular organs and later completed MRI scans of the patient’s brain structure. The data they collected showed that the eye reflexes and perception of spinning lasted a shorter time with the dancers than with the rowers.

From this point, doctors wondered how they could transfer this ability to their patients. After taking an in-depth look at the dancer’s brains it was concluded that the cerebral cortex and cerebellum were the most affected. The cerebral cortex is found in the largest part of the brain and is responsible for speech, judgment, thinking and reasoning, problem-solving, emotions, learning, and the senses. While the cerebellumMajor parts of the brain, a fist-sized portion found in the back of the brain, uses neurons to coordinate voluntary muscle movements and to maintain posture, balance ,and equilibrium. In the AP Biology curriculum, learning the nervous system helps in one’s understanding of transport and membranes. The nervous system sends signals across the plasma membrane of a cell to the brain. With this signal, the cerebellum and cerebral cortex can process information and signal parts of the body to move. From looking at the MRI scans, scientists discovered that the dancer’s cerebellum was smaller. Scientists believed dancers would be better off not using their vestibular system and solely relying on “highly coordinated pre-programmed movements”. Scientists believe it is not necessary for dancers to feel dizziness so, their brains adapted to suppress that feeling. As a result, the signal that goes to the cerebral cortex is reduced. So, if scientists and doctors monitor the cerebral cortex they could begin to understand how to treat patients affected by chronic dizziness.

 

 

NMT5: A New Enemy To SARS-CoV-2?

In the past few months, scientists in the United States have developed a potential new antiviral to SARS-CoV-2.   The drug, called NMT5, is effective against several variants of SARS-CoV-2, the virus that sent the planet into lockdown only a few years ago.

As stated in the journal Nature Chemical Biology, NMT5 coats SARS-CoV-2 particles as they travel through the body.  Thus, when the virus attempts to attach to the ACE2 receptor proteins of the cell, NMT5 attaches first.  The drug changes the shape of the cell’s receptor upon attachment, which makes it harder for SARS-CoV-2 to infect the cell, and on a larger scale, the organism’s body.

In order to ensure that the drug isn’t toxic, researchers tested NMT5 on healthy cells.  According to the National Institute Of Health, it was “found that NMT5 was non-toxic and only changed receptors that were being targeted by the virus. These effects lasted for only about 12 hours, meaning the receptors functioned normally before and after treatment”.  In fact, in an experiment that used hamsters as models for the human immune system, NMT5 reduced SARS-CoV-2’s ability to bond to ACE2 receptors by 95%!

A significant reason NMT5 is so effective is that it not only limits one particle of SARS-CoV-2, but the effectiveness of the virus as a whole, when present. When a SARS-CoV-2 particle with NMT5 attaches to an ACE2 receptor, it adds a nitro group to the receptor, which limits the ability of the particle to attach to the receptor for 12 hours by changing the receptor’s shape.  Thus, no COVID-19 particle can attach to the ACE2 receptor – even ones that haven’t been surrounded by NMT5.  Stuart Lipton, a professor at The Scripps Research Institute, states that “what’s so neat about [NMT5] is that we’re actually turning [SARS-CoV-2} against itself”, as particles surrounded by NMT5 serve to limit the ability of other SARS-CoV-2 particles.  The drug has excited scientists studying SARS-CoV-2 around the world, as they have “realized [NMT5] could turn the virus into a delivery vehicle for its own demise” (PTI, The Tribune India).

Cell reception and signaling are incredibly important to both viruses and the human immune system.  A virus works by infiltrating a cell through cell receptors that line the outside of the desired cell’s phospholipid bilayer.  Viruses attach to these receptors and infect the cell as a result.  SARS-CoV-2’s process is depicted below, as it attaches to the ACE2 receptors described earlier.  The immune system works by recognizing the virus at hand and signaling B-Lymphocytes and T-Lymphocytes to destroy the virus and infected cells.  B-Plasma cells surround the virus, as shown below, which neutralize it and allow it to be engulfed and destroyed by macrophages.  Cytotoxic T-cells kill cells already infected by the virus.  Both B and T Lymphocytes are activated as a result of T-Helper cells, as T-Helper recognize the virus when a piece of it is displayed at the end of a macrophage, and signal the Lymphcytes by releasing cytokines (another example of cell reception and signaling).  This process is all shown in the image below, with the specific virus depicted being SARS-CoV-2.

Fphar-11-00937-g001

However, NMT5 prevents the initial infection from happening when SARS-CoV-2 enters the human body by bonding with SARs-CoV-2 particles before they attach to cells, which allows for the immune system to quickly destroy the virus.  By blocking SARS-CoV-2’s access to receptors, the drug stops the particle before it can infect a cell and do any damage. Since cell receptors are specifically shaped, and any change in form results in a loss of normal function, the ensuing change in shape of a receptor limits any SARS-CoV-2 particle from attaching to said receptor, further limiting the virus’s damage by blocking cell reception from occurring. Thus, the immune system kills the virus without major symptoms.

All in all, the development of NMT5 is exciting for scientists all around the globe.  If it is as effective as studies show, it could play a major role in limiting the effects of SARS-CoV-2.  Hopefully, all goes well, and you should be hearing a lot more about the drug sometime soon.

If you have any updates or questions on NMT5, I invite you to share them in the comments below.  Thank you for reading my blog post, and stay curious!

Is the recently discovered hidden cavity on the SARS-CoV-2 protein a target for drugs?

Many of us have been vaccinated against COVID-19 and have had the virus, leading us to become used to the virus being prevalent in our lives during the past few years. Even though a successful vaccine has been rolling out for a while now, new therapies have not yet been discovered for future strains. Finding new therapies for the virus remains a major priority in the field of science, even if many of us have been protected already. This issue remains a priority because new variants and strains have been continuing to emerge, and some resist present therapy mechanisms.

SARS-CoV-2

The most effective approach to attempting to combat the virus is addressing the proteins on the surface of therapeutic targets, known as spike proteins. The spike protein (S proteins) located on the surface of the virus leads to its spiky protrusions, and its mechanism to enter human cells. Like we learned in AP Biology class, the spike proteins of the virus latch to cells by matching with a specific receptor on a cell’s surface. The spike proteins of the virus have to latch on to the new cell to infect. Successful messenger RNA vaccines properly target this spike protein, which is the main goal when creating new therapies for viruses. 

                                             Spiky appearance of SARS CoV-2 virus

Luigi Gervasio, a chemistry and structural/molecular biology professor at University College London, and his team have been working towards addressing this issue. By partnering with the University of Barcelona’s research team, the two teams took the first steps to discover a possible mechanism for future drugs to detect and protect against the SARS CoV-2 Virus. Through thorough research and investigation, they uncovered a “hidden” cavity on the surface of a prominent infectious agent of the virus known as Nsp1. The team was able to make this discovery by testing small molecules that had the potential to bind to the Nsp1 cavity. The team identified one, 5 acetylaminoindane, which is essential for the development of new drugs against viruses. They concluded that this cavity permitted the calculation of the cavity’s atomically spatial arrangement, which will allow the development of these drugs.

The results of their breakthrough findings set the stage for developing new therapies that will be able to target the NSp1 protein against SARS-CoV-2 and present Nsp1 proteins in future coronavirus strains. Not only will this finding be impactful for targeting SARS-CoV-2 and future variants, but also new cavities on the surface of other proteins that have yet to be found by scientists. Finally, this research is monumental for both SARS-CoV-2 and virus treatment in years to come!  

 

The Science Of Addiction

Overview of the brain

There are three main parts of the brain: the cerebrum, the cerebellum, and the brain stem. The cerebrum controls most of our functions such as movements, thoughts, and even our senses. The cerebrum is roughly two-thirds of the brain as a whole and is divided into four lobes: the frontal, parietal, temporal, and occipital. These lobes control emotions, pain receptors, hearing, vision, and more. Second, the cerebellum is located right behind and a little below the cerebrum, and controls most of our motor functions. Finally, the brain stem is the smallest portion of the brain, sitting beneath the cerebrum and in front of the cerebellum. The brain stem controls both breathing and heart rate, making it just as important as the other parts of the brain regardless of its small size.

Diagram of the brain. Wellcome L0008294

Addiction 

Abusive drugs increase the amount of dopamine in the brain which is produced by the brain stem. Often brain activity that would often be seen from a simple social interaction or through eating food will be seen after addictive drugs are consumed, but the activity will be much more powerful and persistent, leading to the addiction. The brain recognizes the pleasure the drug may grant the user and this numbs the user, over time, to natural releases of dopamine. Further, a study conducted on mice proved that the prefrontal cortex controls social behavior and as social behavior is affected by addiction, one of the major parts of the brain is damaged by drug use.

Connection to biology

The original article articulates how drugs of abuse target circuits in the brain and affect how the reward centers are damaged by drug use. Further, the article focuses on how cortisol levels can affect how quickly a person can recover from an addiction. This is important for addiction research as recovery windows will be more accurate if doctors can test how much cortisol a person has. However, this is not nearly as important as the study of the effects drugs have on our brains. This connects to our biology class so far this year as the plants we’ve been experimenting on in the lab have been watered daily. However, if we suddenly just decided to stop watering them the plants would have the same reaction as someone who was addicted to drugs being cut off: yearning for what was taken from them. In the same way that plants depend on water, a drug addiction makes the addict depend on the drug for functionality as the person’s brain is so damaged that it can no longer produce dopamine without synthetic production through drugs.

Smilies for Article Feed Back

 

Know Someone addicted to Opioids or Painkiller? This Biomedical Advancement May Be Able to Help.

First and foremost, the opioid crisis effects Americans nationwide. The United States is facing a major health crisis that rarely is even mentioned on the news. In the last 20 years(1999-2020) National overdose deaths involving any opioid have risen by more than a factor of six. Nearly 70,000 Americans died in 2020 rising by over 44% since just 2017. Whether given after a major surgery or sports injury, the addictive nature of opioids combined with the difficult side effects have left researchers looking for a better solution.

The general goal for this research was to target different receptors in the cell to do away with the harmful side effects of opioids. An international team of researchers led by the Chair of Pharmaceutical Chemistry at Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU) are “focusing particularly on the molecular structures of the receptors that dock onto the pharmaceutical substances”. In short, they are looking to activate adrenaline receptors instead of opioid receptors.

Researchers looked at the central nervous system to discover receptors in cells that lacked the sedative effect. While many of these adrenaline receptors are involved in pain processing, few have been cleared for use in therapies. This is where a team of researchers from Erlangen, China turned their attention to the adrenaline producing alpha 2A adrenergic receptor. One problem is that the analgesics that target the alpha 2A receptor produce a strong sedative effect. Gmeiner, one of the researchers, quotes “Dexmedetomidine(an analgesic) relieves pain, but has a strong sedative effect, which means its use is restricted to intensive care in hospital settings and is not suitable for broader patient groups”.

The goal for the researchers was to separate the sedative effect from the adrenaline receptors to ensure that this therapy could be used on a wider scale. Through the use of extremely high-resolution cryo-electron microscopic imaging, researchers were able to develop agonists that like Dexmedetomidine send large amounts of adrenaline to the brain thus, revealing  the sensation of pain very well. But, the real development was the “fact that none of the new compounds caused sedation, even at considerably higher doses than those that would be required for pain relief.”

In AP Biology, we have looked at the active transport of molecules through the phospholipid bilayer of the cell. Using ATP energy, cells in your body are able to move particles from a high concentration outside the cell to a lower concentration inside the cell. One process cells use to move these particles is Receptor Mediated Endocytosis. Specific ligands (ions, small molecules, or proteins) bind to a coated pit in the receptor while the receptor matches the ligands shape. Next, the ligands pass through the phospholipid bilayer and are put into a coated vesicle to be transported around the cell. A similar process takes place when receptors receive pain relieving drugs.

The prospect of removing the addictive and violent side effects of opioid use through the use of adrenaline receptors sounds promising, but it is important to keep in mind that this is still just research in the lab. With enough funding and time, the possibility of saving thousands of lives by developing non-opioid pain medication is a very exciting advancement and worth the investment.

Can Reactive Oxygen Species Maintain Stem Cell Function and Prevent Inflammation?

Have you ever wondered what “gut health” really means? What keeps your gut microbiome functioning properly, maintaining homeostasis, and preventing inflammation? Originating from oxygen, reactive oxygen species (ROS) that are highly reactive function as central indicators of cellular flaws and issues in the body, such as inflammation. Nai-Yun Hsu of Mount Sinai has stated that “Reactive oxygen species released by stem cells are critical in maintaining a heathy gut via maintaining proper balance of intestine barrier cell types.”

File:Inflammatory Bowel Disease MTK.jpg 

A team of researchers from the Ichan School of Medicine at Mount Sinai have gone in depth about the importance of these oxygen species for stem cell function, avoiding inflammation, and repairing wounds in a recent study. Using mice as models, the researchers were also able to conclude that microfold cells, called “m cells” regulate an organism’s gut immune response, and emerged from a loss of ROS in mice and humans. 

 

The experiment was conducted in vino and in vitro conditions with the mice cells, and ex vivo conditions with human intestinal biopsies post-colonoscopy. Both the human intestinal biopsies and mouse cells were utilized to determine the amount of ROS in the body to support a finding. In addition to determining the amount of the oxygen species, the biopsies and mice were used to analyze the “gene expression profile” of barrier cells in intestines of mice and humans that are diagnosed with a “subtype of IBD known as ulcerative colitis.”  

 

A decrease in these oxygen species can lead to TNF’s emergence in the body, which is a substance that attempts to maintain homeostasis in the body and avoid inflammatory diseases, like IBD and ulcerative colitis. They have concluded that losing species like NOX1, a protein that creates these species, is directly linked with inflammatory diseases like Inflammatory Bowel Disease (IBD). Judy H. Cho, MD, has stated that the study is a breakthrough “in defining the key role of oxygen species in maintaining a healthy epithelial barrier for IBD.” These reactive oxygen species are relevant to AP Bio considering the information we have learned about general biological systems and cells, which function to maintain homeostasis in the body. The mitochondria, which is an organelle of the cell covered in AP Bio, receives signals from gut bacteria that reveals inflammation. While the mitochondria is typically known as the site of cell respiration and performing reactions, new evidence has shown a relationship between the gut microbiota and mitochondria to trigger immune responses and activate barrier cell function. These processes relate to changes to the mitochondria that occur from gut-related issues in IBD patients, meaning that there is a connection to ROS. 

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Gut Microbiota

As a conclusion to proving the direct link between the highly reactive oxygen species and treating inflammation, these researchers encourage and plan to conduct further study on this topic, but for using “oxygen species-stem cell modulation therapy” to potentially treat IBD patients. 

 

 

CRISPR Gene Editing: The Future of Food?

Biology class has taught me a lot about genes and DNA – I know genes code for certain traits, DNA is the code that makes up genes, and that genes are found on chromosomes. I could even tell two parents, with enough information, the probabilities of different eye colors in their children! However, even with all this information, when I first heard “gene editing technology,” I thought, “parents editing what their children will look like,” and while this may be encapsulated in the CRISPR gene editing technology, it is far from its purpose! So, if you’re like me when I first started my CRISPR research, you have a lot to learn! Let’s dive right in!

CRISPR

Firstly, what is CRISPR Gene Editing? It is a genetic engineering technique that “edits genes by precisely cutting DNA and then letting natural DNA repair processes to take over” (http://www.crisprtx.com/gene-editing/crispr-cas9).  Depending on the cut of DNA, three different genetic edits can occur: if a single cut in the DNA is made, a gene can be inactivated; if two separate DNA sites are cut, the middle part of DNA will be deleted, and the separate cuts will join together; and if the same two separate pieces of DNA are cut, but a DNA template is added, the middle part of DNA that would have been deleted can either be corrected or completely replaced. This technology allows for endless possibilities of advancements, from reducing toxic protein to fighting cancer, due to the countless ways it can be applied. Check out this link for some other incredible ways to apply CRISPR technology!

In this blog post however, we will focus on my favorite topic, food! Just a few months ago, the first CRISPR gene-edited food went on the market! In Japan, Sicilian Rouge tomatoes are now being sold after the Tokyo-based company, Sanatech Seed, edited them to contain an increased amount of y-aminobutyric acid (GABA). “GABA is an amino acid and neurotransmitter that blocks impulses between nerve cells in the brain” (https://www.scientificamerican.com/article/crispr-edited-tomatoes-are-supposed-to-help-you-chill-out/). It supposedly (there is scarce scientific evidence of its role as a health supplement) lowers blood pressure and promotes relaxation. In the past, bioengineers have used CRISPR technology to “develop non-browning mushrooms, drought-tolerant soybeans and a host of other creative traits in plants,” but this is the first time the creation is being sold to consumers on the market (https://www.scientificamerican.com/article/crispr-edited-tomatoes-are-supposed-to-help-you-chill-out/)!

Tomatoes

So, how did Sanatech Seed do it? They took the gene editing approach of disabling a gene with the first method described above, making a single cut in the DNA. By doing so, Sanatech’s researchers inactivated the gene that “encodes calmodulin-binding domain (CaMBD)” in order to increase the “activity of the enzyme glutamic acid decarboxylase, which catalyzes the decarboxylation of glutamate to GABA, thus raising levels of the molecule” (https://www.scientificamerican.com/article/crispr-edited-tomatoes-are-supposed-to-help-you-chill-out/). These may seem like big words, but we know from biology that enzymes speed up reactions and decarboxylation is the removal of carbon dioxide from organic acids so you are already familiar with most of the vocabulary! Essentially, bioengineers made a single cut in DNA inside of the GABA shunt (a metabolic pathway) using CRISPR technology. They were therefore able to disable the gene that encodes the protein CaMBD, and by disabling this gene a certain enzyme (glutamic acid decarboxylase) that helps create GABA from glutamate, was stimulated. Thus, more activity of the enzyme that catalyzes the reaction of glutamate to GABA means more GABA! If you are still a little confused, check out this article to read more about how glutamate becomes GABA which will help you better understand this whole process – I know it can be hard to grasp!

After reading all of this research, I am sure you are wondering if you will soon see more CRISPR-edited food come onto the market! The answer is, it depends on where you are asking from! Bioengineered crops are already hard to sell – many countries have regulations against such food and restrictions about what traits can actually be altered in food. Currently, there are some nutritionally enhanced food on the market like soybeans and canola, and many genetically modified organisms (GMOs), but no other genome-edited ones! The US, Brazil, Argentina, and Australia have “repeatedly ruled that genome-edited crops fall outside of its purview” and “Europe has essentially banned genome-edited foods” (https://www.scientificamerican.com/article/crispr-edited-tomatoes-are-supposed-to-help-you-chill-out/). However, if you are in Japan, where the tomatoes are currently being sold, expect to see many more genome edited foods! I know I am now hoping to take a trip to Japan soon!

Thank you so much for reading! If you have any questions, please ask them below!

How to Keep Your New Year’s Resolutions: The Making and Breaking of Habits

What is a habit? A habit is “a behavior pattern acquired by frequent repetition or physiologic exposure that shows itself in regularity or increased facility of performance“ (Merriam-Webster). With this being the second month of 2022, New Year’s Resolutions are still in many people’s minds. February is statistically the time when individuals give up on their life-changing aspirations that the new-year inspired, “virtually every study tells us that around 80% of New Year’s resolutions will get abandoned around this month” (This Is The Month When New Year’s Resolutions Fail—Here’s How To Save Them). The “new year, new me” mindset is beginning to seem a little too hard to accomplish. If we can create habits that contribute to our new year’s resolutions, maybe they won’t seem so difficult. So, how can we make these resolutions into good habits and break existing bad ones?

New Years Resolutions

Habits are created through associative learning. Essentially, as you repeat a certain behavior in the same context, it becomes an automatic response rather than a thought-out action and that is when it is a habit. When this switch happens, that behavior/action moves from the intentional mind to the habitual mind. So, if we can intentionally make certain changes as a part of a resolution, we will eventually do them without thinking and maybe accomplish a resolution! 

Brain

Now, let’s look at some interesting science involved in the study of habits! Specifically, the dorsolateral striatum. This is a part of the brain that “experiences a short burst of activity” as the brain begins to create a new habit (Revving habits up and down, new insight into how the brain forms habits). As a habit becomes stronger and harder to break, this burst also intensifies. This was proved in an MIT study where rats were taught how to run in a maze and received a sugar pellet reward at the end. As we have learned in biology, neurons are nerve cells that send and receive signals. In fact, we know all about how these signals are transmitted! In this study, using optogenetics, scientists controlled the neurons in the dorsolateral striatum with light. “A flashing blue light excites the brain cells while a flashing yellow light inhibits the cells and shuts them down” (Science Daily). As the rats were running through the maze, if the neurons were excited, they ran faster and habitually, whereas when the flashing yellow light inhibited the cells, the rats slowed down and no longer knew where to go, making wrong turn after wrong turn. Senior author of the study Kyle S. Smith said, “Our findings illustrate how habits can be controlled in a tiny time window when they are first set in motion. The strength of the brain activity in this window determines whether the full behavior becomes a habit or not”. This shows us, it is fairly easy to form habits if you continue it repeatedly as the action first begins! While this can be good or bad, with the other information you will learn in this blog post, I hope that this is encouraging! 

In a recent study rewards were also shown to help form habits. This study explored how giving individuals in India a reward for washing their hands before dinner created good hand washing habits. “The study involved 2,943 households in 105 villages in the state of West Bengal between August 2015 and March 2017. All participants had access to soap and water. Nearly 80 percent said they knew soap killed germs, but initially only 14 percent reported using soap before eating” (Small bribes may help people build healthy handwashing habits). These households were divided into groups. Those that received a reward for washing their hands before dinner did 62% of the time, whereas those who did not receive a reward only washed their hands 36% of the time. This is a big difference! “Significantly, good habits lingered even after researchers stopped giving out rewards” (Small bribes may help people build healthy handwashing habits). Rewards helped create the habit, but once the habit was formed, it was automatic and even without the reward, the habit still took place! Now you may be wondering, why is this information relevant? Well, reward yourself! If your goal is to do one pull-up everyday, give yourself a piece of chocolate every time you do it and eventually you will not need any chocolate! 

So, based on this information, how can we break bad habits? First off, go to a new environment. Due to the fact that habits form from repeated behaviors in the same context, by changing our surroundings, it is much easier to not participate in that behavior. Secondly, repeat a new, replacement behavior over and over. For example, if your goal is to eat less pears, make it a habit to reach for an apple every time you walk into the kitchen. As we know, repetition forms habits! Lastly, keep this new environment and action consistent – don’t start reaching for a banana every time you get home if you have been reaching for an apple when you walk into the kitchen. In order to form a habit it is critical to repeat a certain behavior in the same context. 

Now, we can now create good habits and break the old bad ones! With this information, make this the year that you actually follow through on your new year’s resolutions! Don’t let this month stop you. You have the knowledge and resources, get to it! New year, new you! Good luck! If you have any questions, feel free to comment below!

New Years Resolution

How are new COVID variants identified?

COVID variants are of high concern for scientists studying the disease. Some variants can be more infectious or cause more severe illness. Additionally, some variants can evade vaccines by having different surface proteins than the variant the vaccine was created for. This causes the antibodies produced from the vaccine to be less effective against other variants. In AP Biology class we discussed how the Delta Variant, first identified in December 2020, has a different spike protein structure than the original virus from which the vaccine was created from. This allows the variant to be more infectious, and make the vaccine less effective against it. But, what are COVID variants? And how are they discovered? Hand with surgical latex gloves holding Coronavirus and A Variant of Concern text

COVID variants are “versions” of the virus with a different genetic code than the original one discovered. However, not every mutation leads to a new variant. This is because the genetic code of the virus codes for proteins. Some mutations will not change the structure of the protein and thus not change the virus. So, COVID variants can be defined as versions of the virus with a significantly different genetic code than the original virus.

To detect new COVID variants, scientists sequence the genetic code of virus which appears in positive COVID tests. Scientists look at the similarity of the genetic sequences they find. Then, if many of the sequences they get look very similar to each other, but different to any other known virus, a variant has been discovered.

To sequence the RNA of the virus, scientists use what is called Next Generation Sequencing (NGS). To understand how NGS works, it is best to start with what is called Sanger Sequencing. Sanger Sequencing utilizes a modified PCR reaction called chain-termination PCR to generate DNA or RNA fragments of varying length. The ending nucleotide of each sequence is called a ddNTP, which contains a florescent die corresponding to the type of nucleotide. The addition of a ddNTP also terminates the copying of the particular sequence. The goal of this PCR reaction is to generate a fragment of every length from the start to the end of the sequence. The sequences can then be sorted by length using a specialized form of gel electrophoresis. The sequence is then read by using a laser to check the color of the fluorescent die at the end of each sequence. Based on the color and size, the nucleotide at that position of the genomic sequence can be found.

Sanger Sequencing Example

The difference with NGS is that many sequences can be done in parallel, allowing for very high throughput. In other words, with NGS many COVID tests can be sequenced in once.

The COVID-19 Vaccine: How, What, and Why

We have all seen the news lately – COVID, COVID, and more COVID! Should people get the vaccine? What about the booster shot? Are vaccines more harmful than COVID-19? Will my child have birth-defects? This blog post will (hopefully) answer most of your questions and clear up a very confusing topic of discussion!

Discovery of monoclonal antibodies that inhibit new coronavirus(Wuhan virus)

First off, what are some potential effects of COVID-19? They include, but are certainly not limited to, shortness of breath, joint pain, chest pain, loss of taste, fever, organ damage, blood clots, blood vessel problems, memory loss, hearing loss tinnitus, anosmia, attention disorder, and the list goes on. So, our next question naturally is: what are the common effects of the COVID-19 Vaccine? On the arm that an individual receives the vaccine the symptoms include pain, redness, and swelling. Throughout the body, tiredness, a headache, muscle pain, chills, fever, and nausea can be experienced. To me, these effects seem much less severe than COVID-19’s!

COVID-19 immunizations begin

Now that we have covered effects, you are probably wondering what exactly the COVID-19 Vaccine does – will it make it impossible for me to get COVID-19? Will I have superpowers? Well, you may not get superpowers, but your cells will certainly have a new weapon, which we will discuss in the next paragraph! The COVID-19 Vaccine reduces “the risk of COVID-19, including severe illness by 90 percent or more among people who are fully vaccinated,” reduces the overall spread of disease, and can “also provide protection against COVID-19 infections without symptoms” (asymptomatic cases) (Covid-19 Vaccines Work).

So, how does the vaccine work? Many people think that all vaccines send a small part of the disease into us so our cells learn how to fight it at a smaller scale. However, this is not the case with the COVID-19 vaccine! As we learned in biology class, COVID-19 Vaccines are mRNA vaccines which use mRNA (genetic material that tells our cells to produce proteins) wrapped in a layer of fat to attach to cells. This bubble of fat wrapped mRNA enters a dendritic cell through phagocytosis. Once inside of the cell, the fat falls off the mRNA and the strand is read by ribosomes (a protein maker) in the cytoplasm. A dendritic cell is a special part of the immune system because it is able to display epitopes on MHC proteins on its surface.

Corona-Virus

After being made by the ribosomes, pieces of the viral surface protein are displayed on the surface of the dendritic cell (specifically the MHC protein), and the cell travels to lymph nodes to show this surface protein. At the lymph nodes, it shows the epitope to other cells of the immune system including T-Helper Cells. The T-Helper Cells see what they’re dealing with and create an individualized response which they relay to T-Killer cells that attack and kill virus-infected cells. This individualized response is also stored in T-Memory cells so that if you do end up getting COVID-19, your body will already know how to fight it! The T-Helper Cells additionally gather B-Plasma cells to make antibodies that will keep COVID-19 from ever entering your cells. T-Helper Cells are amazing! As you can see, the vaccine never enters your nucleus, so it cannot effect your DNA! No birth-defects are possible!

You are now equipped with so much information and able to disregard many common misconceptions about the COVID-19 vaccine! Additionally, you can make an educated decision about whether or not you should get the vaccine. I think yes! If you have any questions, please feel free to comment them and I will answer. Thanks for reading!

 

LONG COVID

After the long sufferable weeks from catching COVID-19, you would think you are in the clear; until, that is, you feel some extra “health-issues”. The term for these health issues, specifically after COVID-19, are called Long Covid (post-covid). Generally “one in two [covid recovered people] experienced long-term COVID manifestations” and the symptoms included are a diverse field of sickness. Penn State investigators mentioned the trend of symptoms from 250,351 unvaccinated adults and children:

Loss of General Well Being (weight loss, fevers, fatigue)

Decreased Mobility (1 in 5 experienced a decrease in mobility)

Concentration Issues

Lung abnormalities (6 in 10 survivors tight chests and a quarter of patients had difficulty breathing)

Digestive Issues

What could be the reason that COVID-19 is still lurking around in our bodies when the sickness is gone? Researchers at Yale University studying long-COVID have found a pattern of patients having an “unusual level of cytokines” also known as a cytokine storm. Cytokines are a secreted chemical proteins released by cells for communication. In the Immune System process, after a Macrophage, large phagocytic cells, ingests an antigen it releases cytokines, signaling for a t-helper cell to come. After the helper t-cell recognizes the antigen, more cytokines are released and trigger the Cell-Mediated and Humoral Responses (B and T cells). I mention all this because researchers are saying that post-covid patients tend to have patterns of irregular, more-than average cytokines being produced as well as an “unusual pattern of activity by…t cells. The greater than average amount of cytokines suggests a “state of chronic inflammation” and “kill tissues and damage organs.” The unusual activity of t-cells suggests that COVID-19 could still be lurking in the body.

Cytokine Release

Cytokine release and the numerous amounts of it

The treatment for these conditions are mostly to take the vaccine but there are still many unknowns to this Long-Covid problem. These problems are mostly lying in the Immune System rather than other parts of the body that can be tested with machines; which is why solving this problem is very difficult. This problem can only be solved by a matter of time and hope the scientists can figure this out.

 

The Importance of Gut Health: How to Live Long and Be Happy

Gut health – why is it so important? I had always thought that the concept of good gut health was a myth and only lived on the side of a bottle of Kombucha. I could not have been more incorrect!Kombucha, Health-Ade,

It turns out that a happy gut is critical to live a long, happy, and healthy life! The gut, also known as the digestive tract or gastrointestinal track, includes the mouth, esophagus, stomach, small intestine, pancreas, liver, gallbladder, colon, and rectum. Therefore, it processes all of the nutrients you take in, fights diseases, serves as a center for communication, and produces hormones. These are all critical tasks that affect your everyday well-being!

202004 Gut microbiota

When thinking about gut health, scientists are usually referring to the gut microbiome. In short, the gut microbiome is all of the microbiomes in your intestines. Humans would have a very hard time surviving without the gut microbiome. It digests breast milk when babies are first born, controls the immune system, digests fiber, and even helps control brain health. In fact, a recent study done with mice suggests that gut health affects social interaction/behaviors, stress, anxiety, and autism spectrum disorder. Additionally, in 2011 another study was done with mice, which involved antibiotics killing “bad” gut bacteria, also known as, gut flora. These mice became scientifically less anxious after killing the gut flora and “showed [positive] changes in their brain chemistry that have been linked to depression”  according to Live Science.

Gut flora is not the same for everyone. Another study done with gut flora showed that obese individuals tend to have less diversity in their gut flora when compared to lean individuals. This difference is because of an increase in Firmicutes and decrease of Bacteroidetes in obese individuals. Gut flora also affects an individual’s metabolism because of its affects on the breakdown of a key organic compound we have learned about in biology, carbohydrates. As we know, carbohydrates provide energy for the body which is imperative for all individuals. Another subject we have discussed in our class, amino acids, can have an increase in production because of gut flora (Live Science).

Now, you may be wondering, “how can I keep my gut happy?” The key to a healthy gut comes from diet. After an extensive amount of research, here are some tips I have gathered and why they work:

  1. Eat a variety of foods – to keep your microbiome diverse (recommended to eat specifically a variety of fruits and vegetables for fiber, vitamins, and minerals)
    Fresh fruits and vegetables in 2020 06
  2. Eat fermented foods (ex. yogurt, kefir, kimchi, pickles, sauerkraut) – it “can reduce the amount of disease-causing species in the gut” (Healthline)Vegan yogurt, March 2012
  3. Eat nuts, seeds, and legumes for fiber and proteinNuts on Spice Bazaar in Istanbul 01
  4. Eat whole grains for dietary fiberHome made whole grain bread
  5. Eat prebiotic foods (ex. bananas, artichokes, apples, asparagus, oats, flax seeds, garlic, onions, broccoli) – to “help boost the population and diversity of good bacteria” (Orlando Health)29 Nov 2011 - Apples and BananasThree Onion in Peng Chau
  6. Limit antibiotics – they kill both good and bad bacteria in the gut, which decreases necessary varietyAntibiotic pills
  7. Take a probiotic supplement – it “can help restore the gut to a healthy state after dysbiosis” (Healthline)Red and blue pill

These are all relatively small changes for the huge benefits that they reap. Start incorporating them today to improve your gut health and live a longer, happier, and overall healthier life!

 

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