Stress Doesn't Cause Ulcers, But It Probably Lets It In
Date Posted: August 11, 2026
In 1984, a scientist drank a lab-brewed bacterial culture to prove his theory and won a Nobel Prize for it. For decades, doctors linked ulcers with stress and lifestyle. They had only scratched the surface, missing the bigger picture entirely. Here is the story of how one motivated scientist's self-experiment overturned fifty years of medical belief and why stress still matters in the context of ulcers.
In 1984 Barry Marshall, an Australian physician, drank a lab-brewed bacterial culture. Within days he developed nausea and vomiting. From stomach biopsy, it was confirmed that he had acute gastritis. Instead of being upset, Marshal celebrated this diagnosis, published the results in the Medical Journal of Australia in 1985 (vol. 142, no. 8, pp. 436–439), and even won the Nobel Prize in Physiology and Medicine in 2005. But what made Marshal drink the bacterial mix in the first place?
Marshall’s story is preceded by research and advances in the field of peptic ulcers. Let’s go back around fifty years to a different kind of experiment. In 1930s a young Hungarian-Canadian endocrinologist, Hans Selye experimented with rats, and he theorized that physical stress caused them to develop stomach ulcers. Selye formalized the use of the term ‘stress’ in a physiological context. Medical practitioners linked gastritis with mental stress and the body’s response to stress. The stomach produces acid that helps break down the food. To protect the stomach lining from getting dissolved in the same acid, the stomach also produces bicarbonates to neutralize the acid, and a thick mucus lining to prevent the stomach wall from coming into direct contact with the acid. During long periods of stress, the digestive system is also affected and there is an imbalance in the acid production and the system that protects the stomach. This sometimes causes the stomach wall to encounter acid resulting in stomach ulcers. The treatment at that time focused on reducing acid production and managing stress better.
In 1979, John Robin Warren, a pathologist from the Royal Perth Hospital, was going through biopsy slides when he noticed ‘spiral shaped’ living organisms in the stomach tissues of patients with ulcers. By that time, it had been established that the stomach secretes large volume of acid that makes survival unlikely. Warren was joined by Marshall in 1980s to study these strange bacteria that, against all medical wisdom, survived in stomach acid. In 1983, they published a study claiming that peptic ulcers were related to a bacterial infection rather than production of excess stomach acid. Due to the absence of suitable animal models, Marshall volunteered to drink the bacterial mix and confirmed that the bacteria caused gastritis. This was a paradigm shifting finding, because now gastritis and peptic ulcers could be treated with antibiotics. The ulcer causing bacteria was studied in detail and it was named Helicobacter pylori. It was found that this bacterium can indeed survive in the acidic stomach environment by producing enzymes that neutralize the acid in the small environment around itself. Tests to detect H. pylori in the gut were invented and it was found that most people carry these bacteria, but only a fraction of them develop ulcers. This raised an important question: What is the decisive factor in developing stomach ulcers? This brings attention back to stress.
It isn’t clear how stress increases the chances of developing ulcers but there are some scientifically sound theories. During stress, acid production increases while the mucus lining and bicarbonate become insufficient to protect the stomach wall, allowing lesions and ulcers to form. Stress also reduces immune response to infections as well slows down the repair of damaged stomach walls.
Marshall’s and Warren’s Nobel Prize winning discovery gave a new dimension to approach peptic ulcers, but that does not completely remove the older science linking stress to the disease. In humans, stress alone does not cause ulcers but it makes their occurrence much easier.
Mirror Life: The Reflection That Could Outlive Us
Date Posted: May 12, 2026
What if a single organism that is invisible to the immune system could escape a lab, and spread across the entire biosphere unchecked? This isn’t just science fiction, but close to reality. Scientists are building the components of mirror life, a radical inversion of biology as we know it. What are the ethics and safety considerations behind it?
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You can’t shake your own hands, because although identical, they don’t overlap. In chemistry, some molecules have identical mirror images that do not overlap with each other. Despite having the same structure and physical properties, they can have different biological properties, such as taste or smell. These types of molecules are called ‘chiral’ molecules and each of the identical molecules is an ‘enantiomer’ of the other. The word ‘Chirality’ originates from the Greek word χείρ (kheir), meaning ‘hand’.
As life on earth evolved and complex molecules emerged, biology settled on a single-handedness for all its molecules. As a result, every macromolecule in every living thing shares the same chirality. All the DNA from small bacteria to plants and humans coils clockwise under normal conditions, and the chiral amino acids of the proteins are universally left-handed. The reason why life chose one hand over the other remains an unanswered question in evolutional biology.
This single-handedness of life can have medical consequences. Some drugs are designed to target only one of the enantiomers of the biomolecules. If the mirror-molecule enters the system, the drugs will fail to recognize it and remain ineffective. It is like trying to shake a left hand with a right hand, they just don’t fit.
Scientists are building components to mirror-life, one molecule at a time. So far, mirror-DNA, mirror-machinery to make mirror-RNA from DNA, and mirror-RNA have been successfully reported. These mirror-molecules are very stable and unaffected by natural enzymes that target just the natural biomolecules. The only step missing from establishing life’s central dogma in the mirror-life is the mirror-ribosomes that could translate the mirror-RNA to mirror-proteins. Ribosomes are complex cellular machinery made of proteins and RNA, thus making it an engineering challenge. Once this problem is solved, the mirror-ribosomes would bring mirror-organisms one step closer to reality.
In parallel, scientists are making real progress in synthesizing life of natural chirality from synthetic nucleic acids, proteins, and lipids. Simple reactions between the synthetic biomolecules are established independently, but these haven’t yet been combined into a functioning synthetic cell. Once that is achieved, it would be plausible to follow similar protocols to engineer mirror-life cells. Though it is not an immediate concern, experts across the field of synthetic and evolutionary biology discuss its possibility and consequences. In 2024, a group of 38 scientists published a policy article in the journal Science, calling for careful, coordinated global consideration regarding research in this field and how to prevent it from causing destruction. Notably, they did not call for the research to stop but for oversight, international coordination, and serious public conversation before science outpaces the ethics and safeguards.
A hard question that mirror-life poses is whether it should be made at all. A carefully created mirror-organism could escape the controlled lab environment due to malicious intentions or just human error. In such cases, none of the current enzymes or antibiotics could work against them, and we could face real danger. Science has achieved great heights in advancing medicines, therapeutics, astrophysics, and every other field, and it has the potential to grow more. But if we do not tread carefully, the same science could risk everything that we have achieved so far. The question is not whether scientists can make mirror-life but whether we are wise enough to contain it.
Epigenetics: You are more than your DNA
Date Posted: April 27, 2026
Your DNA isn't your destiny. The Dutch Hunger Winter showed how famine epigenetically reprogrammed unborn children, leaving chemical scars that caused metabolic disease decades later. Epigenetics switches genes on or off without altering DNA itself. However, unlike DNA, epigenetics can be revered through lifestyle choices and emerging therapies.
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In September 1944, Nazi Germany imposed a food blockade on the occupied Netherlands, starving 4 million Dutch residents in the winter. Many people lost their lives to food shortages before the blockade was finally lifted the following May. This clear start and end date of the famine and confined geographical region created a natural (but sad) human experiment. The unborn children of pregnant women who were unfortunately exposed to the stress of food scarcity grew up to be individuals suffering from Type 2 diabetes and heart issues. ‘Dutch Hunger Winter’ became a widely studied subject in the field of prenatal malnutrition and its long-term effects.
DNA sequences make ‘genes’ that govern our physical features and health. Epigenetics is a change in gene activity without affecting DNA itself. Lifestyle choices such as food, exercise, or chronic stress can determine if parts of the DNA will be expressed or silenced. The DNA sequence is the same in each cell of the body. Other factors sit on top of the DNA that control its expression. This is why the brain can think, the eyes can see, and the gut can digest the food, even though the DNA in all their cells is the same. The cellular environment attaches a chemical group (methyl) to the DNA nucleotides, which stops the DNA expression. The gene is still present, but the cellular machinery ignores it.
During the politically induced famine in the Netherlands, the fetuses in their first 10 weeks were preparing for a world with food shortages. This caused epigenetic reprogramming, which affected the glucose tolerance in the body by storing all the sugar and fat. However, when these fetuses were born, the famine was over, and there was no longer any food scarcity. Their prenatal environment did not prepare them for food abundance, which led them to develop chronic metabolic diseases even six decades after their birth. The striking part of this study was that the ‘chemical scar’ made in the first trimester of conception remained unaffected even when they grew into elderly adults.
Unlike DNA, the epigenetic markers are not permanent. A class of epigenetic therapies works by reversing its effects. They do not change the underlying DNA but alter the level of DNA methylation to change what parts of DNA are read. There is also evidence showing that healthier habits produce beneficial epigenetic changes. The epigenome is a live conversation between the body and the environment, and Science is getting closer to joining it to prolong a healthy life.
Date Posted: April 15, 2026
The Gila monster, a large venomous desert lizard, has played an unlikely role in the development of modern diabetes medicines. A fortunate side effect of these treatments was significant weight loss in patients, which opened an entirely new therapeutic avenue for these same drugs. The pharmaceutical industry has since been engineering new molecules to make administration more convenient for patients, with the latest breakthrough being a once-daily oral pill. Read further to understand the science behind these drugs.
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All the food that you eat goes through a journey in the body, where it is broken down into sugar molecules that float around in the bloodstream. This provides energy for activities, from moving to thinking. But what happens when you skip a meal? The sugar supply drops, but you remain functional. Insulin, a hormone produced in the pancreas, binds with the sugar in the bloodstream and stores it in cells. This sugar reserve ensures a steady release of energy even when there is no food. In some people, this insulin system fails either because the body does not respond to insulin as it should or the pancreas does not produce enough insulin. This causes blood sugar to remain high for a long time, eventually leading to type 2 diabetes. Treating diabetes requires managing blood sugar levels with insulin medication. Insulin cannot be taken as an oral pill because the strong acids in the stomach would destroy it before it reaches the bloodstream, making it an injectable medication. It also requires extra measures, such as planned meals, continuous blood sugar monitoring to prevent life-threatening low blood sugar, and side effects such as weight gain. This called for an alternative diabetes treatment.
In the 1990s, New York-based endocrinologist John Eng was studying unknown hormones and their functions. He came across an unlikely reptile- the Gila monster, a large venomous native to the deserts of the southwest of North America. Like many reptiles, Gila monsters can go for months without food. What sets them apart from other reptiles is that their blood sugar levels stay stable during fasting. This immediately made a connection with diabetes patients who face problems regulating blood sugar.
Eng’s studies on Gila monsters’ saliva revealed a molecule named exendin-4, which is structurally very similar to another molecule in humans, named Glucagon like peptide-1 (aka GLP-1). In humans, GLP-1 binds to GLP-1 receptors. Yes, an admirable lack of effort given to names. Exendin-4 and GLP-1 have similar functions- triggering insulin release, slowing digestion, and suppressing hunger. One difference between these two molecules is their half-life. Half-life is related to the time a molecule spends in the bloodstream before it gets destroyed or removed. Exendin-4 could last for hours, but GLP-1 lasted just a few minutes.
From a pharmaceutical perspective, if the half-life of GLP-1 could be increased, it would trigger insulin production for a longer time. This would manage the blood sugar levels and ultimately diabetes. This new category of drugs will be called GLP-1 receptor agonists. Eng patented his discovery and sold the license to a pharmaceutical company. The first GLP-1 receptor agonist drug, named exenatide, was available to patients in 2005 as a twice-daily injection. Ouch! Since then, there have been efforts to make the administration of drugs more convenient.
Currently, two of the most popular drugs, named tirzepatide and semaglutide, are available as once weekly injections. The patients’ blood sugar levels were responding well to these drugs and never went life-threateningly low. The researchers studying these patients noticed an unexpected effect of the drugs. The patients started losing significant amounts of weight!
This was the beginning of another direction for the same GLP-1 receptor agonist drugs- weight loss. However, the weekly injections remain inconvenient and unpleasant for many people, creating a demand for a pill that could do the same job. One company modified the GLP-1 structure further and packed it in a pill that could be stored at room temperature. This drug is absorbed poorly in the gut, so the pill needs to be taken on an empty stomach. Another company went in a different direction. Instead of modifying the natural hormone GLP-1, they synthesized a completely new molecule, named orforglipron. It behaves like GLP-1, binds to the same GLP-1 receptors, triggers insulin release, and eventually leads to weight loss. This pill can be taken at any time of the day without dietary restrictions.
GLP-1 receptors are present not just in the gut but in other organs as well, like the brain, heart, and kidneys. The story continues, with researchers now exploring whether these drugs could have benefits beyond weight loss, like reducing cardiovascular risk, treating addiction, and neurodegenerative diseases. The unlikely Gila monster from the desert might have led the way for groundbreaking medicinal discoveries.
Date Posted: April 5, 2026
Large Language Models (LLMs) are becoming increasingly popular among digital creators and writers for drafting content, editing, and conducting research. While they can generate fluent and convincing text, they lack true understanding. In scientific fields like computational biology, they can assist learning but cannot replace precise simulations or expert analysis. Read ahead to learn how most LLMs are trained and why can not be relied upon for scientific accuracy.
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The training of Large Language Models (LLMs) can be broken down into three simple steps.
Step 1, Reading existing texts: LLMs are provided with freely accessible texts such as books, blogs, news articles, Wikipedia, open-access research, and even unfiltered Reddit conversations. However, they cannot access texts behind paywalls. LLMs "read" these to find common patterns, such as which word is most likely to follow another. With a large amount of training data, they develop vocabulary, learn to connect context across different prompts, and string together pieces of text that can sound like a "new idea." This is also how LLMs can write code in programming languages without being explicitly taught the basics of programming.
Step 2, Learning the right kind of response: Once trained on data, an LLM can respond to a prompt in unpredictable ways, without any sense of whether a response is offensive, unhelpful, or accurate. For example, if asked about the fruit "orange," the LLM might generate text about other fruits or drift into discussing the color. In this step, human trainers provide examples of good, helpful responses so that the LLM learns to follow instructions and stay on topic.
Step 3, Learning what humans like: Finally, human evaluators rank multiple LLM responses from best to worst. This teaches the LLM to respond in ways that users find helpful and trustworthy. It also makes LLM responses sound confident.
After the three stages of training, the LLM is ready to generate responses that "sound good” but that does not mean they are correct. LLMs cannot understand “truth”, and their responses can sound confident even when they are factually wrong. This is known as hallucination, and this is why LLM responses should not be trusted for scientific, medical, or legal matters.
In fields such as computational biology, accuracy isn’t optional. Molecular modelling and simulating biological processes take time and expertise. The LLM can summarize and teach complex molecular dynamics, but it is incapable of computing quantitative parameters or independently running the simulations.
LLMs are one corner of a much larger AI landscape. Other tools, like AlphaFold, are built for very different purposes. AlphaFold is a protein structure predicting software that is trained on physical and biological data. It uses the patterns in the data to predict structures of proteins. AlphaFold won the 2024 Nobel Prize for Chemistry for solving the 50-year old 'protein folding problem'. However, it predicts just one structure instead of full conformational landscape and dynamics. This is where a computational biologist can provide complete insight into biomolecular dynamics, interactions of molecules and prediction of behavior across environments.
Advances in AI can accelerate scientific discovery by automating analysis and uncovering patterns in complex data, but computational researchers remain irreplaceable, bringing the critical thinking and expertise that transforms results into meaningful science.
Date Posted: March 27, 2026
Project Hail Mary is a sci-fi film based on Andy Weir's novel of the same name. It explores one of humanity's most profound questions: are we alone in the universe? If other life forms exist, how would they compare to us in intelligence and complexity? The story follows Ryland Grace, a scientist and reluctant astronaut, on an interstellar journey full of extraordinary discoveries. The science behind the story is not too far beyond reality. Here are some illustrations explaining the science of Project Hail Mary.
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The premise of Project Hail Mary revolves around a unicellular extraterrestrial life form called Astrophage. These organisms survive and ‘feed’ on the surface of stars and travel to carbon dioxide-rich planets to reproduce. Although astrophage is fictional, real-world parallels exist on Earth that can survive in extreme conditions. Extremophiles are organisms that survive in environmental conditions that are extreme or hostile to humans, like hot thermal vents of volcanoes, concentrated salt lakes, high-pressure ocean trenches, or high radiation environments. One such extremophile is tardigrade (also known as water bear), which can survive in some extreme environments. Experiments during space missions have shown that a significant population of tardigrades survive vacuum of space and intense solar radiation. They show resilience against extreme cold, but sustained heat kills them. Apart from heat, they also have natural predators such as mites, spiders, and worms.
The storyline’s main conflict stems from the absence of predators capable of controlling the population of astrophages. Uncontrolled proliferation of astrophages would lower the energy of the sun, with apocalyptic consequences for life on Earth. Introducing predators in the astrophage biosystem would keep its population in check, saving the sun from cooling. Such predator-prey relations (wolves-deer) also maintain a healthy ecosystem on Earth.
Finally, the story touches on the theory of panspermia. It hypothesizes that life originated in space and was brought to Earth by comets, radiation or intentional seeding by more intelligent species. Since there is no conclusive evidence of extraterrestrial life, panspermia remains just a hypothesis. Project Hail Mary is an interesting read (and movie) that imagines the universe with different life forms or varying intelligence and complexities.
PS for fellow scientists who have watched the movie: That centrifuge scene annoyed me as well!
Date Posted: March 14, 2026
The immune system is one of nature's most sophisticated defense mechanisms, but sometimes it gets things wrong. A drifting pollen grain, a trace of peanut, or a new medication can trigger a full-scale immune reaction that manifests as allergic symptoms ranging anywhere from a runny nose to anaphylaxis. Why does your own body turn against you, and what can you do about it?
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After the holiday season, you start the new year and get back to work with full gusto. You are excited about the days getting longer and the weather getting warmer. The trees and grass are blooming, bringing back color, but also with it, your seasonal allergies. And just like that, the season you've been waiting for turns on you with puffy eyes, a relentless runny nose, and sneezes that won't quit.
Allergies occur when the immune system mistakes harmless things (like pollen, dust, or certain foods) as a threat, triggering a cascade of chemicals that produce symptoms. The immune system is made of different types of cells that work in sync. They work as the body’s defense mechanism that protects against severe diseases by fighting off pathogens. On the first encounter with a pathogen, the immune system produces antibodies to recognize it and eventually neutralizes it. During future attacks by the same pathogen, the body is already prepared to fight it quickly. This is the same principle behind vaccination. The immune system is introduced to versions of pathogens, so it is ready to fight the real infection.
Why does the immune system turn against you, giving you anything from a runny nose to a life-threatening emergency?
In people with allergies (or hypersensitivity), the same immune system misfires. Depending on the type of immune response, hypersensitivities are classified into four types. The most common type of hypersensitivity is Type I, which is characterized by the presence of IgE antibodies. This type of hypersensitivity is casually termed as ‘allergy’, and symptoms arise within seconds to minutes of allergen exposure. On the first contact with an allergen, there are no symptoms, but the immune system produces IgE antibodies to recognize the allergen. These antibodies bind to mast cell surfaces, the body's first line of contact with allergens. On subsequent allergen exposure, the mast cells recognize them and release a cocktail of chemicals, most prominent being histamine. Histamine recruits the entire immune system to address the perceived threat, triggering the onset of allergic symptoms. Anaphylaxis is an extreme case of Type I hypersensitivity where mast cells from many organs release histamine, simultaneously increasing the scale and speed of the reaction. The histamine dump causes blood vessels to dilate, airways to constrict, and blood pressure to plummet.
In Type II hypersensitivity, the immune system produces antibodies to kill other cells in the body. Most commonly, drugs cause Type II allergies. In the bloodstream, drugs bind to the surface of cells, and the immune system fails to recognize the drug-coated cell as one of the body’s cells. These ‘foreign looking’ cells are tagged by the antibodies released by the immune system. This triggers the ‘kill’ signal that destroys the antibody-tagged cells and sweeps them away from the system.
Type III hypersensitivity occurs when the immune system encounters foreign substances (new medication, animal-derived treatments such as antivenoms) in the bloodstream and releases many antibodies. These antibodies bind to foreign substances, forming large immune complexes that are not cleared away easily and accumulate in the tissues and blood vessel walls surrounding healthy organs. While clearing these immune complexes, parts of the healthy tissue also get damaged, causing fever, pain, rash, and kidney inflammation. Type III hypersensitivity is not immediate, and the symptoms occur after a few hours. This makes the diagnosis tricky, as the delay in the onset of the symptoms makes it difficult to connect it to the cause.
All the hypersensitivities mentioned above involve some kind of antibody produced by the immune system. In Type IV hypersensitivity, antibodies are not involved; a different type of cell (T cell) is directly involved. Just like Type I, the first exposure to allergen sensitizes the T cells, without causing any symptoms. Any future exposure recruits the T cells to produce immune signals (cytokines) that trigger localized inflammation. Since there are no pre-formed antibodies, the symptoms take 2-3 days to develop. Such type IV hypersensitivities can cause a rash to develop after contact with nickel jewelry, latex, or certain cosmetic products.
Do antihistamines work for all allergies?
Antihistamines (OTC brand name: cetirizine, loratadine) can manage symptoms that arise from histamines, that is, only Type I hypersensitivity. They are most effective if taken before an allergen exposure or right at the start of the allergic reaction. The speed of anaphylaxis requires the administration of epinephrine (EpiPen), which overrides all the physiological signals and reverses all the symptoms of anaphylaxis. For the other types of hypersensitivity, the best remedy is to remove triggers and suppress the immune response using corticosteroids. Contact rashes in Type IV can be managed by applying corticosteroid topical creams. Types II and III require systemic administration orally (drug: prednisone) or intravenously.
Is there any other treatment for allergies?
Antihistamines and corticosteroids suppress the immune response caused by allergies. These work fine for mild symptoms, but for life-threatening instances such as anaphylaxis, it is better to look for more sustainable remedies. Allergen immunotherapy, commonly known as allergy shots, gradually desensitizes the immune system through controlled and repeated exposures. This is the closest thing to a long-term cure for allergies that is currently available at an affordable cost.
Is an allergy the same as intolerance?
Some people experience intolerance to certain foods, such as lactose or alcohol. The main difference between allergy and intolerance is the involvement of the immune system. For intolerance, the immune system is not involved. It is important to know the difference between the two so that proper care can be made available in times of need. Someone with lactose intolerance lacks the enzymes needed to digest dairy products, causing an uncomfortable but harmless digestive issue. However, milk allergy could trigger a serious immune response, creating a life-threatening emergency.
Allergies are not just an inconvenience to endure. They are a well-understood immune response that can be managed, treated, and in some cases, overcome.
Date Posted: March 9, 2026
Phone batteries don't just drain faster, they are chemically affected. Extreme heat and cold affect phone batteries differently, with some effects reversible and others permanent. Electric vehicles face the same challenge with the same battery technology, so how do they manage to keep going where phones fail?
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You hiked for an hour in the cold to reach the top of the hill, which is covered in fresh and crisp snow, and the sun is making everything glitter. You take out your phone to capture the aesthetic view, only for it to die on you when you need it the most! Not just that, the phone battery also drains faster if you hike on a hot summer afternoon. Like us, phones also hate extreme temperatures and age with time.
Batteries are energy storage devices for electricity. When you charge a battery, it converts the electricity into chemical energy and stores it until you need it. All batteries, whether used in remotes, mobile phones, or electric cars, have the same construction. They have two electrodes (named anode and cathode) and an electrolyte in between.
Phones use Lithium-ion batteries that have graphite (anode) and Lithium-cobalt-oxide (cathode) as the electrodes and a Lithium salt in organic solvent as the electrolyte. It also has a porous plastic material to prevent short circuits between the two electrodes and protect it from thermal runaway (like the phone catching on fire). In a fully charged state, lithium ions are concentrated at the graphite anode by intercalating into the graphite structure. During phone use, they migrate from the anode to the cathode through the electrolyte, while the electrons move through the electronic circuit and power the phone. When the phone is plugged in, the lithium ions migrate back from the cathode to the graphite anode, restoring the charged state. Although the main chemical reaction recharges the phone battery, other side reactions physically damage the battery. The Lithium ion, instead of intercalating in the graphite, sometimes gets deposited on the surface of the graphite anode. This creates an irreversible layer of Lithium atoms on the anode (lithium plating). Over time, charging-discharging cycles create a thick layer that permanently consumes the Lithium atoms, thus reducing the battery's performance. The electrolyte also breaks down and gets deposited over the graphite layer, increasing the battery’s resistance.
At cold temperatures, the organic solvent in the electrolyte becomes more viscous, slowing down the movement of the Lithium ions and the electrons. This increases the resistance of the phone battery, and it does not read the voltage (charge percentage) accurately. This causes the phone to slow down or die on the spot, but it recovers as soon as it is put in a warm pocket. When the phone heats up during use, charging, or on a hot summer afternoon, the rate of all chemical reactions increases, discharging the battery quickly. The unwanted reactions, like breaking down the electrolyte, also increase damaging the battery irreversibly.
Lithium-ion batteries are not just used in phones, but also in electric vehicles. Unlike phones, the performance of vehicles is not drastically affected by driving in extreme temperatures. This is due to the inbuilt battery thermal management system (BTMS) that regulates the temperature in the proximity of the battery. Since phones are not equipped with such systems, you can feel the dramatic effect of temperature.
Unfortunately, modern phone batteries are glued to the phone. When the battery gets old and its performance degrades, the entire phone needs to be replaced. However, this is not the end, and we can look forward to improvements in battery technology that can be lighter, longer-lasting, and cheaper to manufacture. Until technology catches up, rely only on your eyes and mind to capture the glittering snow, and not on the cold phone.
Cortisol: Built for predators, stuck with deadlines
Date Posted: March 3, 2026
Cortisol gets a bad reputation as the 'stress hormone', but it quietly runs much of your daily life, from waking you up to keeping you alert. Cortisol evolved to save us from predators, and millions of years later, it's still running the same program. Except now, the predator is a work email on the weekend, triggering the release of cortisol and keeping us up at night.
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Often referred to as the ‘stress hormone’, cortisol has other roles to play. It is responsible for waking you up in the morning, regulating metabolism and blood pressure, and keeping you alert. Cortisol follows a 24h cycle, peaking and dipping throughout the day. Its level starts rising in the early morning (around 2-3 am) and peaks in the morning to wake you up. It gradually decreases during the day and reaches the lowest level at midnight, when your body relaxes into sleep. A slight increase in cortisol level can affect these peaks and dips. During periods of stress, this early morning slow rise of cortisol is enough to wake you up. This is why sleep feels fragile during times of stress. You wake up around 3 a.m. and can’t get back to sleep. All because of the cortisol that is trying to get you ready for the day.
During any ‘external threat’ (being attacked by a lion, going down on a roller coaster, or seeing a work email on a weekend marked ‘urgent’), the brain fires up signals in two phases, 1) the fast neuronal signal that takes seconds, and 2) the slower hormonal signal that takes a few minutes. Both signals reach the adrenal gland and produce two hormones- adrenaline (fast) and cortisol (slow). Adrenaline causes the immediate ‘fight-or-flight’ response, increasing the heart rate and sweating. Cortisol that is released in minutes maintains the high energy level. It temporarily slows down non-essential functions like digestion, growth, immune response and reproduction. It prioritizes supplying energy over storing it. It releases stored glucose and increases blood sugar level, so that the brain and muscles have enough energy to deal with the ‘external threat’.
Once the threat passes, cortisol does not get cleared away immediately. The half-life of cortisol (the time in which cortisol levels to reduce by half) is around 60-90 minutes, taking time for the levels to return to normal. This is why you feel alert and unsettled after a stressful event has passed. After reaching the normal level, the organs and systems affected by the increased cortisol revert to their regular functioning.
Cortisol is an important hormone evolved to protect against natural threats like running away from predators or falling off cliffs. However, modern-day stress has a slow-burning effect and never seems to go away. Continuous stress from work, financial worries, unexpected life-changing events, or the news keeps your body in a state of ‘threat’. This creates a continuous increase in cortisol, leading to sleep disruption, indigestion, a compromised immune system, and brain fog. Over time, chronic stress and high cortisol often lead to anxiety, heart disease, and depression.
The functioning of cortisol hasn’t changed in thousands of years, but the world that we live in has changed. Although you don’t have an apex predator chasing you down the road, you do have worries about job security or loans. Stress throws the cortisol clock out of sync, leaving you tired and feeling miserable. Simple lifestyle changes like regular exercise, prioritizing good sleep, and limiting artificial light can reduce the ‘stress’ signal and keep excess cortisol in check.
The Rise of Superbugs: Understanding Antibiotic Resistance
Date Posted: February 25, 2026
Less than a century ago, Penicillin changed medicine forever. Infections that once killed could be cured with a pill. But now, the bacteria are fighting back. Antibiotic resistance is turning our most trusted medicines into ineffective drugs. How do antibiotics work, and can we stay ahead of the bacteria outsmarting them?
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Penicillin was discovered in 1928 as a drug that kills bacteria. It took years of research before it could be mass-produced and made commercially available by 1945. Penicillin revolutionized the field of medicine and saved lives by killing the root cause of infectious diseases such as scarlet fever, pneumonia, syphilis, and other infections resulting from open wounds. Modifications to the chemical structure of penicillin led to the development of a class of penicillin-type antibiotics that are more effective against a wider range of infectious bacterial species. It has been less than a century since the discovery of penicillin, and now we see bacteria evolving to be resistant to antibiotics.
How do antibiotics work?
Bacteria are unicellular organisms. In most cases, bacteria survive in colonies where they exchange information via chemical signals. Antibiotics attack the parts or the functions of the bacteria that are responsible for their survival.
Disrupting cell walls: Some bacteria have cell walls that protect them against physical stress. Drugs like penicillin disrupt the cell walls and prevent their rebuilding. This causes the bacteria to swell up and ultimately burst. However, not all bacteria have a cell wall and they remain resistant to penicillin. It is important to know the kind of bacterial infection before treatment with penicillin.
Blocking essential functions: All living cells, including bacteria, have cellular machinery that produces and recycles complex molecules like proteins and nucleic acids. A certain class of antibiotics blocks the bacterial cell from performing these essential functions by binding to the machinery. Bacteria develop resistance to these antibiotics by actively pumping drugs out, producing chemicals that attack the drug itself, or changing the working of their machinery.
Leaking cellular content: Cell membranes are made of lipid bilayers that keep the aqueous interior of the bacterial cells from leaking out. Some antibiotics act like detergents, damaging the cell membrane. The bacteria rapidly lose important ions and molecules, leading to their death. Such antibiotics cause physical damage to the cell membrane. It is difficult to develop resistance to these antibiotics as it would require the bacteria to rebuild the entire cell membrane. Although this class of antibiotics is the last resort against antibiotic-resistant bacteria, some of these drugs are known to cause kidney problems.
Why is antibiotic resistance a global threat?
Antibiotic resistance is a result of evolution and natural selection. In all living systems, random mutations occur regularly. Some of these mutations have an advantage and function better than others in surviving. These mutations get passed on to further generations. Bacteria in large colonies also undergo similar mutations. Some of these mutations help them survive against antibiotics. Since bacteria have a short lifecycle, these mutations occur and are passed on very quickly to new generations, giving rise to "superbugs" that are resistant to almost all antibiotics. Bacteria also have a unique way of sharing pieces of genetic information with other members of the colonies. Consequently, the existing bacteria also develop resistance.
Misuse of antibiotics without identifying the causative bacteria, not completing the full antibiotic dose, and overuse of antibiotics in agriculture and livestock are major reasons leading to antibiotic resistance. Bacterial infections spread easily from one place to another via air, water, the food supply chain, and human travel. Antibiotic resistance is particularly problematic as it cannot be contained in one area and is a rising global concern.
Do we have an escape plan?
The rapid rise of antibiotic resistance is a race against time. Without new technology, we risk returning to a pre-penicillin world, where even minor cuts could result in deadly infections. Greater awareness is needed across hospitals, pharmacies, and educational institutions to ensure antibiotics are prescribed at the appropriate dose and duration, and only when clinically justified. Regulatory reforms are needed in countries where antibiotics are available over the counter, often at low doses. Without proper identification of the bacterial strain, such low doses risk prolonging illness and worsening its severity. Meanwhile, alternatives such as bacteriophages, which selectively destroy bacteria without harming human cells, and membrane-disrupting peptides are emerging as promising solutions.
All these approaches cannot eliminate the occurrence of antibacterial resistance, which is a natural process. We just need to slow the spread long enough for science to develop the next generation of treatments.
Is Your Thyroid Calling for Attention?
Date Posted: February 17, 2026
The thyroid gland controls metabolism and mood through a hormonal feedback loop. When this loop is disrupted, it leads to hypothyroidism or hyperthyroidism, causing symptoms like weight changes, fatigue, and anxiety. What disrupts this loop, how are these conditions diagnosed, and how are they treated?
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Feeling low, tired, and noticing sudden weight gain? Chances are, it’s not your lifestyle, but your body’s biology that needs attention!
The thyroid is a small, butterfly-shaped gland in the neck above the collarbone that plays a major role in metabolism and mood regulation. It produces two hormones, triiodothyronine and thyroxine, commonly known as T3 and T4. (Yes, these are the ones reported in blood work.) The numbers 3 and 4 refer to the number of iodine atoms in each hormone. That’s why iodine is important for healthy thyroid function. The thyroid produces almost 20 times more T4 than T3. T4 is converted into T3 inside tissues. The amount of T4 and T3 in the bloodstream signals the pituitary gland in the brain to produce thyroid-stimulating hormone (TSH, also reported in blood work). TSH tells the thyroid how much T4 and T3 to produce. This forms a feedback loop between the pituitary and thyroid glands to control T3 and T4 levels in the body.
In certain cases, malnutrition, hormonal imbalance, and inflammation affect the feedback loop between the pituitary and thyroid. The thyroid gland produces either too much or too little of the T3/T4 hormones. Low T3/T4 level (called hypothyroidism) causes an increase in TSH and slows down metabolism, causing sudden weight increase and tiredness. Other symptoms include dull skin, hair fall, irregular menstrual cycle, mood changes, sensitivity to cold, and constipation. To test hypothyroidism, the hormone levels of T3/T4 and TSH are measured. Once confirmed, the patient is prescribed an appropriate dose of synthetic T4 hormones (levothyroxine) to compensate for the lack of natural T4 in the body. This brings back the feedback loop in the normal range, and the symptoms of hypothyroidism disappear.
In the opposite case of overproduction of T3/T4 by the thyroid gland, called hyperthyroidism, the body’s metabolism increases, causing the patient to lose a lot of weight, experience anxiety, insomnia, and heat intolerance. The excess T3/T4 production causes the pituitary gland to decrease TSH, which shows up in the blood work. To bring back the feedback loop to normal, the patients of hyperthyroidism are prescribed Methimazole, which blocks the production of T3/T4 hormones by the thyroid gland.
Thyroid function is also affected by autoimmune conditions such as Hashimoto’s and Grave’s disease. Hashimoto’s is a common cause of hypothyroidism in people with sufficient iodine intake. In this condition, the body produces antibodies (Anti-thyroid peroxidase (Anti-TPO) and/or Anti-thyroglobulin) that attack the thyroid gland, thus decreasing the production of T3/T4 hormones and increasing TSH. Hashimoto’s is confirmed by blood work showing the presence of the Anti-TPO antibodies in the blood. It is not a life-threatening condition and can be easily managed with levothyroxine medication.
In Graves’ disease, the immune system produces antibodies against the thyroid gland, such that it does not recognize the TSH that is secreted by the pituitary gland. This causes an overproduction of T3/T4, leading to a decrease in TSH and causing hyperthyroidism. Graves’ disease is confirmed by the presence of TRAb and TSI antibodies, which affect the TSH sensitivity of the thyroid gland. Grave’s disease can be managed by taking Methimazole in a proper dose, which stops the production of T3/T4 by the thyroid gland.
The thyroid gland may be small, but it plays a major role in keeping the body functioning. Thyroid issues related to it remain one of the most underdiagnosed issues, with women at a high risk of developing thyroid issues throughout their lifetime. The good news? Once diagnosed, most thyroid problems can be managed with proper medication. If you experience symptoms like tiredness, sleep problems, or unexplained weight changes, do not dismiss them as age or stress related. See your doctor and get your bloodwork done- your body might be calling for attention and proper care.
Spatial omics: The (W)hole in one
Date Posted: February 12, 2026
Spatial omics maps biomolecules within tissue to reveal how cells interact and function. Three key techniques, (i) sequencing, (ii) fluorescence microscopy, and (iii) mass spectrometry, offer different ways to profile RNA, proteins, and epigenetic markers. Combined with AI-driven analysis, spatial omics is advancing disease diagnosis and enabling personalized precision medicine.
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Spatial omics profiles biomolecules by their location in tissue. This spatial data reveals new insights into intercellular interactions and signaling. In the last decade, spatial omics has become popular with disease researchers and has enabled many commercial brands. Three main analytical techniques offer varied biomolecular coverage and spatial resolution: Next Gen Sequencing (NGS), microscopic imaging, and mass spectrometry.
The NGS methods can spatially map the transcriptome (RNA expression) on a tissue sample. The RNAs from the tissue conjugate to complementary DNA fragments on a slide that act as spatial barcodes. The spatially barcoded RNAs are then amplified and sequenced. During the data analysis, the whole transcriptome can be mapped back to specific regions of the tissue using the barcodes. With new advancements, NGS-based transcriptomics can be combined with proteomics and epigenomics (DNA and histone modifications) to study mechanisms of health and disease.
The microscopy-based omics methods use fluorescence signals from targeted biomolecules as a readout of their quantity and spatial coordinates. The biomolecules of interest (RNAs or proteins) are sequentially imaged using fluorescence in situ hybridization (FISH). For transcriptomics, DNA strands labelled with a fluorophore are introduced into the sample. They bind to their complementary RNAs only, which are imaged using a fluorescence microscope. Before continuing with the next round of imaging, the previous fluorophores must be removed to avoid false readings. This is achieved by either photobleaching the fluorophores or stripping away the fluorophore-labelled DNA. For proteomics, proteins are immunolabelled with antibodies. The secondary antibodies are generally tagged with barcoded DNA strands.
Another technique for spatial proteomics uses mass spectrometry in combination with a microscope. Proteins on the tissue are marked using metal ions tagged to antibodies. Then, a laser ablates the sample at the precise location of the metal atom, and it is detected using a mass spectrometer. Alternatively, laser-assisted microdissection can isolate specific regions of interest from a tissue, and these samples can be further analyzed for proteomic studies.
All these methods produce large data sets. With the fast-paced development of AI-based platforms, one can perform complex data analysis, improve data quality, and integrate different datasets. It can produce a final image or a 3D model with colocalized information from the multimodal spatial omics. Such studies have potential in translating into clinical applications for disease diagnosis, monitoring, and designing personalized precision medication for patients.
Spatial omics has come a long way since pathologists inferred spatial context in tissues primarily using H&E staining. Today’s state-of-the-art spatial omics are rapidly growing to facilitate understanding of human health and the molecular mechanisms of sustaining life.