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Noah Whiteman, professor of evolutionary biology at UC Berkeley, writes about how toxins are repurposed into medicines for Issue 06. Whiteman’s recent book is called “Most Delicious Poison.”

When you hear the word "poison," perhaps you picture a Victorian-era cobalt bottle labeled "NOT TO BE TAKEN" or the iconic pictogram of a leering skull and crossbones. What probably does not come to mind, however, are the dried white beans in your kitchen pantry, the molluscs who once lived in cone shells in your bathroom jar, or the Botox injection that magically erased your facial lines. Yet, as an evolutionary biologist and geneticist who studies co-evolution between species, I think of these and more.

Now, don't worry. The way we typically prepare white beans completely deactivates the mild toxin that could otherwise cause food poisoning, the highly venomous cone snail that produced that shell was long gone by the time you picked it up, and Botox has been safe to inject by licensed healthcare professionals since FDA approval in 1991. All are examples of compounds we have not only learned to attenuate but actually use to our benefit.

The toxins they make fall into a class of biological molecules known as peptides or proteins. Both form from chains of amino acids — proteins often consist of more than 1,000 amino acids, while peptides typically contain fewer than 100. These amino acid chains have been used for eons by all cells for essential biological functions, such as transporting materials around the body or catalyzing chemical reactions. Additionally, many can be used as weapons by their bearers — either defensively or offensively — to cause pain, tissue damage, paralysis, emaciation, or even death. These abilities are precisely what make them promising as potential therapies, particularly as we find ways to enhance their safety profiles. Botulinum toxin (Botox) from bacteria is one such familiar example.

While small-molecule drugs continue to play a critical role in modern medicine, we are witnessing a shift toward the increasing development of amino acid-based therapeutics. Toxic peptides and proteins, particularly from the venoms of animals, are predicted to be a major source of next-generation peptide and protein-based drugs.

The prominence of these drugs has risen further still with the phenomenal success of semaglutide (sold as Wegovy and Ozempic). While these and other peptide-based drugs weren’t patterned directly on molecules from venoms, many rely on some of the natural mechanisms by which toxins operate. A closer look at these evolutionary templates reveals why inspiration from nature’s “poisonous proteins” will continue to drive drug development.

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Peptide-Based Drugs

Sessile organisms, whether a sponge, coral, plant, or mushroom, are often quite literally between a rock and a hard place. They cannot jump, run, swim, or fly away from danger if a hungry animal wants to take a bite out of them. To counteract this vulnerability, evolution has driven these stationary creatures to produce myriad toxins that act as chemical defenses.

In plants, remarkably, a set of these toxins includes amino acids that mimic the normal amino acids needed by our cells to make proteins. When these non-proteinogenic amino acids are incorporated into proteins, they cause them to malfunction. For example, some legume plants make L-canavanine, which is a bitter and toxic molecular mimic of the amino acid L-arginine. Herbivorous animals that consume L-canavanine-bearing plants produce misfolded proteins by incorporating the mimic instead of L-arginine, rendering the resultant protein useless to the cell.

It isn't just herbivores that get tricked by non-proteinogenic amino acids; humans do, too. In Into the Wild, John Krakauer chronicled the life and death of Chris McCandless, who traveled to the Alaskan wilderness to “find himself.” McCandless survived by foraging for food, inadvertently consuming the poisonous seeds of the legume Hedysarum alpinum, known as Alpine Sweet Vetch. Krakauer and his scientific collaborators determined that the seeds of this species contain high levels of L-canavanine. This unsuspected addition to his diet may explain the last selfie he took shortly before his death, which captured an emaciated shell of a man. Of course, the plant didn’t evolve L-canavanine to kill humans specifically, but any seed-eating predators.

While these toxic non-proteinogenic amino acids seem to have evolved as plant defense mechanisms, pharmaceutical scientists have repurposed them as broader tools in drug development. Rather than using them as toxins per se, the researchers have cleverly turned the tables by incorporating non-proteinogenic amino acids into therapeutic peptides and proteins. This approach is helping to solve rapid degradation by the body, one of the biggest challenges in amino acid-based drugs.

One example of a drug that uses such a mechanism to hinder its own degradation is the anti-diabetes and anti-obesity “wonder drug” semaglutide. This class of drugs was engineered to mimic the body’s glucagon-like peptide-1 hormone (GLP-1), which decreases blood glucose levels by activating its receptor to signal the release of insulin. Scientists at Novo Nordisk ingeniously replaced a critical amino acid that appears early on in the peptide sequence with a non-proteinogenic amino acid. This replacement prevents the peptide from being degraded by dipeptidyl peptidase-4, an enzyme our cells normally produce. This resistance to enzymatic degradation allows semaglutide to persist in the body over days instead of mere hours.¹

GLP-1 receptor agonists work, in part, by triggering the release of insulin from the pancreas. Insulin was the first peptide licensed as a drug in 1922, and while we don’t usually think of it as a toxin (outside of its occasional use as a murder weapon, as in the film Reversal of Fortune), it is a formidable one — especially in certain species. If you live in or have visited the Indo-Pacific region, you may have seen the striking dappled shell of the geographer cone snail, Conus geographus, a marine snail that feeds on fish, washed up on the beach. These shells must be collected with great care as, if one has an occupant, it is one of the most toxic animals on Earth.

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Cone snails, all 600 species or so, prey on marine animals, from other snails and worms to fish. An exquisite set of adaptations has allowed this slow-moving mollusk to catch faster prey. Chief among them is a peptide released into the water by the snails that forms a poisonous cloud — that peptide is a specialized insulin found in this chemical cloud called "nirvana cabal." Once the fast-acting insulin is in the water, it enters the gills of unsuspecting fish and causes a plunge in blood sugar levels or hypoglycemic shock.

Stunned, the poisoned fish fall to the ocean floor, where the snails are waiting to pull them in with their net-like mouths. The insulin released into the water is a near-perfect molecular match of the insulin produced by the fish to regulate their blood sugar, an example of convergent evolution, or the re-evolution of the same trait in different species. Nirvana cabal insulin was first discovered in 2015 and, in 2022, was modified into a drug called mini-Ins, a fast-acting, minimal human insulin analog being pursued to treat diabetes.

Hundreds of additional peptide-based toxins are found in species of cone snails that subdue their prey more directly. These ambush predators kill fish by launching a harpoon-like proboscis and injecting a venomous cocktail. Its components, aptly named “conotoxins,” operate very differently from nirvana cabal. Due to binding to channels, transporters, and receptors in nerve cells involved in pain, the peptides that comprise most conotoxins have tremendous pharmaceutical potential — and thousands of varieties, from α-conotoxins to ω-conotoxins, are predicted to have evolved in cone snails. One of these drugs represents a class of peptides more complex than any mentioned thus far, cyclic peptides.

Cyclic Peptides

While peptides aren’t as long and intricate as proteins, they can fold on themselves to create cyclic peptides with novel modes of action. The pain medicine Ziconotide is one such molecule, developed from a toxic cyclic peptide found in the venom of the cone snail Conus magnus by the lab of Dr. Baldomero Olivera, who grew up in the Philippines, exploring the tidepools where these snails live. Ziconotide and its natural analog are composed of three peptide rings and work by blocking the voltage-sensitive calcium channels that activate our nerve cells, inhibiting pain. Far more potent than opioids, this natural peptide-based drug is now being used experimentally to treat severe chronic pain.

A far more well-known cyclic peptide is found in a group of innocent-looking white mushrooms that may even grow on your lawn. Alpha amanitin is the potent poison produced by mushrooms in the genus Amanita, which include the "death cap" and "destroying angel," or "angel of death" mushrooms. These species are responsible for most poisonings and deaths following mushroom consumption worldwide because many edible mushrooms resemble the deadly Amanita. Between 10 and 20 percent of cases prove fatal.

Alpha amanitin is composed of eight amino acids. This deadly structure allows it to kill its victims by preventing their cells from making messenger RNA (mRNA) through inhibition of the enzyme RNA Polymerase II. Without mRNA, there is no "message" for our cells' ribosomes to translate into peptides or proteins by linking together amino acids. Without new peptides and proteins, the cells die.

Remarkably, certain insects have evolved to feed only on "the angel of death" and its toxic relatives. Biologist Dr. John Jaenike discovered that species of Drosophila flies that normally feed on these mushrooms have adapted to be insensitive to alpha amanitin, while those like the laboratory animal model fly D. melanogaster, which usually feeds on brewer's yeast, are killed by it. The mechanism for alpha amanitin resistance is as yet unclear, but could provide the basis for an antidote.

The genes that encode the enzymes to make alpha amanitin have moved between distantly related mushrooms through a phenomenon called horizontal gene transfer (HGT). HGT occurs when a gene is naturally spliced into the genome of one species from a distant relative. Viruses and selfish genetic elements called transposons, or "jumping genes," are the genetic scissors and glue that cut and paste a gene from one species’s genome to another. If a gene transmitted by HGT happens to make it into the DNA of a cell that leads to the production of sperm or eggs, it then passes into the offspring and can be leveraged by natural selection if it enhances the fitness of its bearers. Alpha amanitin confers a huge benefit, protecting mushrooms from all but the few specialized invertebrates that have managed to pierce the toxic shield.

Alpha amanitin might, like linear peptides and other cyclic peptides like the conotoxins, hold promise as a potential drug. Alpha amanitin is being studied as a type of antibody-drug conjugate (ADC), which programs an antibody to home in on cancer cells while carrying a toxic small molecule payload capable of being imported into the cancer cell and killing it. Around 15 ADCs are currently on the market (although none yet use alpha amanitin as the toxic payload). The ADC approach allows healthy cells to avoid the deadly effects suffered by the cancer cells as their RNA polymerase II enzymes are shut down. Researchers have proposed using alpha amanitin as just such a Trojan horse to fight pancreatic cancer.

Even more structurally complex peptides are found in diverse snake venoms around the world, a rich source of drugs approved by the U.S. Food and Drug Administration (FDA) and the European Medicines Agency (EMA). The saw-scaled viper from Africa, Central Asia, and South Asia provides tirofiban, which is an antiplatelet drug used to treat acute coronary syndrome (the sudden blockage of blood flow to the heart) patterned after the venom peptide echistatin. A similar drug, Eptifibatide, patterned on a venom component in the same family as echistatin, is from the venom of Barbours pygmy rattlesnake from the southeastern U.S.

Finally, anfibatide, from the sharp-nosed viper of China and Taiwan, is a promising anti-coagulant drug that has been evaluated in a Phase IIb clinical trial. This drug binds to the human platelet glycoprotein Ib α-chain involved in clotting and brings us to the next class of poisonous proteins, the lectins.

Lectins

Lectins bind to sugar molecules and often serve as receptors, distinguishing “the self” from pathogen molecules. Like other amino acid-derived compounds, lectins can be toxic — some so dangerous they're classified as "select agents" by the U.S. government due to terrorism concerns.

The most notorious of these is a lectin domain of the toxin ricin. Ricin is made by the castor bean, which is not a legume but a spurge (in the same Euphorbiaceae family as poinsettias), often used as an ornamental plant. Notorious alleged assassinations and assassination plots have involved ricin. The most infamous allegedly occurred in 1978 on Waterloo Bridge in London. Bulgarian Georgi Markov, a critic of the Warsaw Pact, was reported to have been shot in the leg with a small metal pellet thought to contain ricin fired from a modified umbrella. Although the means of his poisoning were never proven, Markov died four days later.

Ricin is toxic because it inactivates ribosomes, RNA-protein machines that translate each triplet codon of mRNA into its corresponding amino acid, linking them together to form peptides and proteins. This is the step after the initial transcription of DNA into mRNA by RNA Polymerase II, the protein to which alpha amanitin binds. In both cases, peptide and protein production stops. Unable to make peptides and proteins, we die. The family of proteins that includes ricin is aptly called "Ribosome-Inactivating Proteins" or RIPs (scientists who study poison have been known to enjoy a little macabre humor). While ricin may be the most famous of these toxins, the lectins found in uncooked legumes, like phytohemagglutinin, which can cause food poisoning, are among the most ubiquitous.

Exploiting the potent cell-killing potential of RIPs, researchers have developed another Trojan-horse immunotherapy able to deliver ricin-based toxins to cancer cells. Additionally, a ricin-based immunotherapy called T-Guard was part of a Phase III clinical trial to treat Steroid-Refractory Acute Graft-vs-Host Disease, which is a common disease emerging after hematopoietic stem cell transplant. Although some safety concerns recently halted this particular application, T-Guard is now being studied as a potential treatment for systemic sclerosis, an autoimmune disease affecting 1.47 million people worldwide. By targeting the problematic, activated immune cells underlying this disease, T-Guard therapy has the potential to reset the immune system without requiring higher-risk stem cell transplants.

Peptides, both linear and cyclic, as well as the more complex carbohydrate-binding lectin proteins, are all passive toxins. But the truth is that ricin actually is built of two domains: one domain is a lectin that passively binds to its target, and the other domain is an enzyme that actually hydrolyzes the ribosomal RNA, thereby inactivating the ribosome. So, rather than simply binding to components of cells or their products, this other class of proteins, called enzymes, repeatedly catalyze chemical reactions and thus are used to disrupt vital biological processes of the cell again and again. The shift from passive toxins to active, reusable toxins represents another successful evolutionary weapon system that pharmaceutical researchers are learning to harness.

Enzymes

Perhaps the most toxic protein enzyme of all is botulinum toxin. Botulinum toxin, produced by Clostridium botulinum, works by being transported into nerve endings at the junctions between muscles and motor neurons, where the toxin prevents the release of a critical neurotransmitter, acetylcholine, into the space between the nerve cell and muscle cell. Without acetylcholine, the muscle cell receives no signal, resulting in paralysis. The evolutionary advantage the bacteria gain by producing this toxin is unclear. However, one theory is that by paralyzing animals, the bacteria rapidly divide and can maximize their odds of dispersal to a new host by hitching a ride on the blowflies and other insects attracted to the fresh carcass.

Botulism was once a major public health problem, mainly through infected wounds and undercooked or poorly preserved food. The heightened susceptibility of babies to botulism is why honey, which is sometimes found to contain this bacterium, is not advised for infants. Botulism may be most familiar in the context of canned food, but high heat easily destroys the protein, just as it does the phytohemagglutinin (a toxic lectin) in raw or undercooked beans.

Frighteningly, one gram of purified botulinum toxin could kill upwards of one million people, which is why the authorities are so concerned about its potential use as a bioweapon. Botulism antitoxin, the only antidote, is derived from antibodies from horses injected with the toxin and must be administered quickly (within 24 hours) because it can only bind to toxin that has not yet bound to the cellular targets.

The pharmaceutically promising aspect of this deadly protein is that it can relax muscles. Botulinum toxin has the temporary effect of smoothing out facial wrinkles, making it useful in cosmetic applications. In 2020, 4,401,536 doses were given by physicians to patients in the U.S. alone for cosmetic, minimally invasive procedures. The global market was valued at $6.1 billion in 2022 and is expected to grow to $11.5 billion by 2031. The toxin provides more than just aesthetic medicine. It also treats muscle spasm disorders, including eyes that are out of alignment (strabismus), chronic migraines and other headaches, excessive sweating, overactive bladder, pelvic floor dysfunction, cerebral palsy, temporomandibular joint disorders (TMJ), and premature ejaculation. Botulinum toxin injections have also been found, inadvertently, to ease symptoms of depression, although the mechanism is not yet known.

While the botulinum used for Botox originally evolved in bacteria, the neuromuscular junction is a popular target for protein-based venom components from other organisms. One is the Thai cobra. This remarkable snake has two options for defending itself with its protein-based venom. It can spit it into its victim's eyes or deliver it into the bloodstream through a bite. Cobratoxin is the main protein in the cobra's venom, and unlike botulinum, which prevents the release of acetylcholine through enzymatic action, cobratoxin binds directly to the nicotinic acetylcholine receptors. The result is similar to the effect of Botox. If hit in the eyes, temporary or permanent blindness can occur, and if a person is bitten, unless the antivenin or CPR is administered, death by asphyxiation ensues as the diaphragm becomes unable to contract.

There is a flip side to cobratoxin. Researchers have shown that it can alleviate pain in laboratory animals and may have potential as an anesthetic. In China, cobratoxin is approved for use as a pain reliever for moderate to severe pain, although this use is not without risks, such as respiratory arrest.

Some creatures have evolved to use a combination of the above-mentioned strategies. The venom from Lonomiacaterpillars, belonging to the silk moth family, is incredibly complex and includes components that run the entire gamut of amino acid-based molecules, from peptides to lectins and enzymes, and more. Lonomia larvae release their venom when someone (or something) inadvertently brushes up against them. Because the caterpillars are gregarious and form clusters when resting on tree trunks or moving across the forest floor, many hairs from many different caterpillars break off at the same time, simultaneously envenomating any unlucky passerby.

When a hollow hair penetrates the skin, venom peptides and proteins move into the blood and spread throughout the body. The peptides and proteins then activate the clotting response, which malfunctions. Victims die of massive internal bleeding, sometimes slowly, over several days. There is an antivenom, produced from the venom of one Lonomia species, but it must be administered within 24 hours, and it is unclear how well it works in other Lonomia species. Fortunately, less than 1 percent of reported Lonomia stings prove fatal now that there is antivenom available for at least one species, although in Brazil from 2007-2018, there were 6,636 reported envenomization events, 1,484 of these cases received anti-venom treatment, and 12 people died. In fact, in Brazil, the case fatality rate from Lonomia stings is three to four times higher than for snake bites.

In 2021, Ornithologist Dr. Carlos Daniel Cadena, Dean of Science at Universidad de los Andes in Bogotá, introduced me to his colleague Dr. Camila González-Rosas, who studies these toxic caterpillars in South America, where they kill several people every year. Since then, working alongside Dr. González-Rosas, my team and I have been using modern genomics to understand how these peptides and proteins evolve to produce the multi-pronged toxicities of Lonomia’svenom.²

Like the other toxins we’ve discussed, the peptides and proteins in the venom of Lonomia species are being explored as potential therapeutics for a diverse array of pathologies. Our hope is that the genome sequence of the Lonomia species we are characterizing will further the development of antivenoms and cures.

A Toxic Two-Step

While tidepooling for venomous cone snails in the Philippines or gathering caterpillars in the Colombian jungle are exotic ways of finding the next breakthrough peptide or protein-based drug, my lab also studies a system closer to home. It lurks amongst the watercress, a mustardy green, growing on the Berkeley campus just 100 feet from my laboratory.

Dwelling there are tiny leaf miners (fly larvae) that tunnel into the watercress leaves, eating them from the inside out. These flies, called Scaptomyza flava, are closely related to D. melanogaster, a premier animal model of human biology. My lab is interested in how the flies evolved to feed in a living leaf because it is such a different environment from the rotting fruit on which they more typically feed. Pertinent to us, the living watercress leaf is trying to kill them by means of chemical defenses, like mustard oils (which trigger our wasabi receptor).

In our search to understand how S. flava evolved from their fruit fly ancestors, my former PhD student noticed that one gene in S. flava’s genome was an outlier. It didn’t seem to belong to a fly’s genome but to a bacterium’s. Yet, the gene had been happily residing in the fly’s genome for millions of years. Around 25 million years ago, S. flava’s ancestors “borrowed” this gene from bacteria and their viruses, called bacteriophages.

This relates to our story of “poisonous proteins” because the protein encoded by this gene, Cytolethal distending toxin subunit B (CdtB), is an enzyme that gets secreted by the bacteria and taken up by animal cells those bacteria infect. After entering the cell, CdtB acts like a DNA scissors and cuts the molecular threads. The broken DNA spills out into the cell, triggering apoptosis, or programmed cell death. This CdtB enzyme is an endonuclease, in the same class as the Cas enzymes used in CRISPR systems.

What is S. flava doing with this incredibly toxic enzyme in its cells? After all, the CdtB toxin evolved to harm animal cells for the bacterium’s benefit, but now it is actually being produced by an animal. It turns out that S. flava makes the CdtB enzyme in its immune cells, which secrete it into the blood of the fly, where it targets the cells of their major enemy: parasitoid wasps. These wasps are the main infectious enemies of insects and inspired the Xenomorphs in the movie Alien.

By borrowing a poisonous protein from the bacteria and their viruses, S. flava did an evolutionary end-run around the wasp, neutralizing this foe. What is more, we found that the same gene had independently moved from bacteria and their viruses into the genomes of many other insects, including the fruit fly Drosophila ananassae, which ultimately proved easier for my team to study than the S. flava.

We found that when we experimentally mutated the CdtB gene from the D. ananassae genome using CRISPR so it didn’t encode the CdtB protein anymore, the flies were more susceptible to attack by parasitoid wasps. Then, we moved the gene encoding the CdtB enzyme to the genome of the D. melanogaster fruit fly, which doesn’t normally have it. When that fly expressed the enzyme in immune tissues, it became instantly resistant to the wasps. But when we expressed it in every cell of the fly’s body rather than just the immune tissues, the flies died. This told us two things: first, that the jumping genes could instantly benefit the fly, but only if the fly expressed the enzyme in the right cells; second, it could also kill the fly if it was produced throughout the fly’s body.

As it turns out, the version of CdtB we discovered may have potential as a template for drug development. First, it may serve as yet another Trojan horse, entering cancer cells and cutting their DNA, causing them to die. Alternatively, cancer cells that evolve resistance to radiation therapy might be made susceptible again by combining radiotherapy treatment with DNA-damaging CdtB from bacteria.

The D. ananassae version of the CdtB toxin is actually fused to a different toxin component called Apoptosis Inducing Protein of 56 kilodaltons that helps the toxin move through the fly’s blood and reach the wasp egg within. It appears to be a toxic, fusion protein new to science. Because this novel version of CdtB borrowed from bacteria has evolved in the immune systems of animals (the flies) for millions of years, it is likely to have properties that are more amenable for use as a therapeutic in humans than bacterially-derived CdtB.

Time will demonstrate whether our work is of more than just academic interest, but like all of the protein-based drugs I've discussed here, these molecules emerged through the crucible of natural selection. Their potential as therapeutics exists precisely because of how they evolved as the result of intense ecological pressure between species.

Casgevy, for example, is the first CRISPR cure for sickle cell disease. It arose eons ago in the battle between bacteria and bacteriophage. Researchers modified the bacterial CRISPR-Cas9 adaptive immune system against phages by optimizing it to recognize the DNA sequence of only the faulty hemoglobin gene. They added the non-sickling DNA sequence from the hemoglobin gene as a template alongside the toxic, DNA-cutting bacterial Cas9 enzyme and the RNA guides that allow it to recognize the precise hemoglobin DNA sequence that needed editing, and in so doing, replaced the sickling hemoglobin sequence with the non-sickling one. In the end, these scientists had transformed an ancient bacterial defense mechanism that relies on a “poisonous protein,” the Cas9 enzyme, into a targeted therapeutic tool. This exemplifies how we can enhance natural molecular weapons through strategic engineering while preserving their core evolutionary advantages.³

While such therapies are a small but growing fraction of modern medicine, there is no question that AI and computational approaches have already greatly accelerated their discovery. Presumably, with targeted training, AI will become better at emulating the process of evolution itself, or more specifically, understanding the chemical co-evolution between species that gives rise to the toxin and resistance mechanisms that we see in nature. By training AI to watch for and simulate chemical co-evolution using genome sequences across the tree of life, we hope to increase our ability to more rapidly generate novel defense and counter-defense molecules in silico. By embracing bio-inspired design, wherein computation is combined with evolutionarily-inspired models, we can expect ever-greater therapeutic efficacy and precision.

As we usher in such technology, the longest-running and most productive R&D laboratory remains nature's own, active for 4.5 billion years. The process of evolutionary adaptation has created precise chemicals, evolved to target specific molecules with minimal off-target effects, a quality that the pharmaceutical industry spends billions of dollars engineering. In his chapter on antibiotics from his book The Invention of Surgery, author David Schneider dismisses the notion that most of our life-saving medicines are designed in some corporate drug office. Here he captures the very essence of my work: “Pharmaceutical scientists rely on billions of years of evolution among the tiniest inhabitants of our world, deciphering which molecules have novel methods of defense and confrontation and utilizing these newcomers in the battle of our attackers.”

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Noah Whiteman is a professor of genetics, genomics, evolution, and development at the University of California, Berkeley, where he teaches and leads research on chemical co-evolution between species. His fascination with toxic organisms began during childhood explorations in Minnesota's boreal forest and has taken him from the Galápagos Islands for his dissertation research to the molecular biology laboratories of Harvard, and eventually Berkeley, where he studies how species evolve to produce and resist deadly chemicals. He received a Guggenheim Fellowship to write "Most Delicious Poison: The Story of Nature's Toxins–from Spices to Vices" (2023) and was awarded the 2025 Genetics Society of America Medal for his team’s discoveries on the genetic mechanisms underlying evolution’s chemical arms race.

Cite: Whiteman, N. “Toxic Proteins for Drug Discovery.” Asimov Press (2025). https://doi.org/10.62211/62gj-94ku

Acknowledgements. Former Postdoctoral Fellow Dr. Samrhidi Chaturvedi (now at Tulane University) and PhD student Diler Haji are leading the sequencing of the Lonomia species in collaboration with Dr. González-Rosas and her team. Former Ph.D. student Dr. Kirsten Verster (now at Stanford University) and current PhD student Rebecca Tarnopol led the studies on CdtB. Julie Johnson from Life Science Studios illustrated the cone snail and death cap drawings. Collage by Ella Watkins-Dulaney.

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Footnotes

1. While semaglutide is the current cause célèbre among therapeutic peptides, the power of GLP-1 mimicking drugs was first realized in a hormone isolated from the venom of the Gila Monster, a large lizard that lives in the Sonoran Desert. Owing to the unpredictability and harshness of that environment, these lizards are the ultimate intermittent fasters. They can go months at a time between meals, necessitating keeping their metabolism and blood sugar levels low.
2. Venoms vary between Lonomia species, including their physiological effects, and this is important for designing anti-venoms that work broadly.
3. Recently, researchers used AI to screen an antimicrobial peptide library for candidates that interfere with a virulence factor produced by the bacterium that causes Huanglongbing, or citrus greening disease. When they treated infected trees with these candidates, severity of symptoms was lessened, providing hope for a beleaguered agricultural sector.