Last year’s Chemistry Nobel Laureate has co-authored a groundbreaking study published in Nature that could transform the treatment of snakebites. The research introduces innovative proteins capable of neutralizing lethal toxins found in snake venom, offering a potentially safer and more effective alternative to traditional antivenoms.
The World Health Organization estimates that venomous snakebites affect 1.8 to 2.7 million people annually, leading to around 100,000 deaths and three times as many long-term injuries, including amputations. Most incidents occur in Latin America, Asia, and Africa, where limited healthcare infrastructure exacerbates the problem.
Currently, antivenoms are derived from animal plasma—a method that is not only costly but also prone to side effects and limited efficacy. Different snake species produce vastly different venoms, further complicating treatment, especially in regions with diverse snake populations. However, advances in understanding snake venom and counteracting its effects are opening new avenues for treatment.
A Leap Forward with AI-Driven Protein Design
Led by Timothy Patrick Jenkins from DTU Bioengineering and David Baker, the 2024 Nobel Laureate in Chemistry from the University of Washington, the team used deep learning technologies to develop synthetic proteins that specifically bind to and neutralize toxins from venomous cobras.
Promising Results in Early Testing
The study focused on a notorious class of snake venom proteins called three-finger toxins, which are known to render traditional plasma-based antivenoms ineffective. While the AI-designed proteins cannot yet neutralize entire snake venoms—which are complex mixtures of various toxins—they provided full protection against lethal doses of three-finger toxins in mice, achieving survival rates between 80% and 100%, depending on the dose and toxin type.
“These toxins are particularly challenging because they often evade the immune system, making plasma-based therapies unreliable,” said Susana Vazquez Torres, lead author of the study and researcher at the University of Washington. “Our work shows that AI-driven protein design can overcome these challenges.”
David Baker highlighted the practical advantages of this approach:
“The antitoxins we’ve developed are discovered entirely through computational methods. They’re inexpensive to produce and have proven robust in laboratory tests.”
Expanding Access to Treatment
The researchers believe that synthetic proteins offer several advantages over traditional antivenoms. Unlike plasma-based antivenoms, which rely on immunizing animals, these proteins can be manufactured using microbes, potentially lowering production costs and making treatments more accessible to low-income regions.
Timothy Patrick Jenkins noted additional benefits:
“These designed proteins are exceptionally small, which means they’re likely to penetrate tissues more effectively and neutralize toxins faster than traditional antibodies. Plus, using AI-powered tools significantly shortened the discovery process.”
A New Era for Drug Development
While standard antivenoms will remain the primary treatment for snakebites in the near term, the team envisions their AI-designed proteins as complementary therapies that can boost the effectiveness of existing treatments. In the longer term, these innovations could pave the way for entirely new classes of antitoxins.
Beyond snakebites, the researchers see broader applications for their protein design approach. “This method could help tackle diseases that currently lack effective treatments, such as certain viral infections,” said Baker. “By reducing the time and cost required for drug discovery, we can make high-quality medicines more affordable and accessible—especially in resource-limited settings.”
The study’s findings mark an exciting step forward, offering hope not just for snakebite victims but for broader advancements in medicine.
Source:
Journal reference:
Torres, S. V., et al. (2025) De novo-designed proteins neutralize lethal snake venom toxins. Nature. doi.org/10.1038/s41586-024-08393-x.