This de novo approach, creating proteins not found in nature, stands apart from most antivenom research, which typically targets single species or toxin types. This approach used Claude Science, a large language model, to generate protein sequences without relying on existing natural structures as templates, a departure from traditional antivenom development.
The team’s work, documented in a report available via the WHO website, focused on creating binders through computational design and subsequent experimental validation. The design process involved setting specific rules for protein structure and function, then allowing Claude to generate candidate sequences, as outlined in the supplementary information.
De Novo Proteins Neutralize Lethal Scorpion & Snake Toxins
S. Ahmadi and colleagues demonstrated nanobody-based recombinant antivenom effective against cobra, mamba, and rinkhals bites, while M. D. Overath’s team showed in vivo protection against cobra venom neurotoxicity with de novo single-domain antibodies. These designs move beyond traditional antivenom development, which often relies on pre-existing antibodies or laborious screening processes. Jeon and colleagues detailed an agentic campaign control for high-throughput binder design, while Latent-Y, an autonomous agent, further automates the de novo drug design process.
Kim and Romero benchmarked the behavior of these LLM agents, assessing their performance in protein design tasks. Xu and colleagues developed ProteinMCP, an agentic AI framework for autonomous protein engineering. Several approaches are being explored to enhance these designs, including BoltzGen and BoltzDesign1, which aim to improve binder design through novel algorithms.
J. Butcher and colleagues expanded the capabilities of RFdiffusion3 to design all-atom biomolecular interactions, while Y. Cho and colleagues used structure hallucination within diffusion models for protein design. Candido and colleagues reported a language model materializing a world model of protein biology, suggesting a deeper understanding of protein interactions is emerging.
RFdiffusion and ProteinMPNN Enable De Novo Protein Binder Design
Analysis of 211 tested designs revealed that 64 pairs were identified as hits at one laboratory or both, and further categorized to understand binding characteristics. Despite this setback, other research groups continue to advance protein binder design, with methods like PXDesign, Genie 3 and Odin-Multi offering modular and accurate approaches.
BindCraft2, an easy-to-use suite, provides tools for designing a wide range of protein binder modalities, while researchers are also exploring methods to accelerate open-source biomolecular models using Claude, as outlined in a September 2026 technical report. These parallel efforts suggest a many-sided approach to addressing the complex problem of venom neutralization.
Claude Science Drives Autonomous Binder Design Campaigns
The team documented these campaign details, including prompt specifications and Claude’s subsequent decisions, in a technical report available through Hugging Face datasets. Structural insights into scorpion venom neutralization are expanding beyond traditional antibody studies, with research detailing the atomic-level interactions between toxins and their targets. L. Riaño-Umbarila et al. demonstrated the structural basis of neutralization of Centruroides noxius venom by a human-derived single-chain antibody fragment.
Cross-Reactivity in Antibody Fragments Neutralizes Scorpion Venoms
A 2001 study in European Journal of Biochemistry characterized a single-chain antibody fragment that neutralized toxin AahI from Androctonus australis hector venom, establishing the feasibility of targeting specific toxins with engineered antibody fragments. Serrumab, a human monoclonal antibody, countered both the biochemical and immunological effects of Tityus serrulatus venom, according to a 2014 publication in Journal of Immunotoxicology. Researchers also investigated strategies to improve antibody persistence, with a 2012 mAbs study outlining a method for mitigating fast clearance rates, a critical factor for effective in vivo protection.
Serrumab & Single-Chain Antibodies Show Toxin-Neutralizing Capacity
At Adaptyv Bio, four such antibodies, 9004G, LR, RU1 and 9C2, showed mean apparent dissociation constants (Kd) ranging from 18 to 66 nanomolar against Ts1. M. B. Pucca et al. reported that Serrumab, a human single chain- fragment antibody, demonstrated nanomolar affinity for multiple scorpion toxins, registering a Kd of 1.9 nM by SPR. UniProt data for the toxins, Cn2, Ts1, AaH II and AaH I, were used, with mature chain lengths ranging from 61 to 83 amino acids.
Neglected Tropical Disease: Urgency for Scorpion Antivenom Research
This finding emphasises a critical gap in public health resources and research directed towards these often-overlooked envenomations, despite their significant impact on morbidity and mortality. Anthropic, in collaboration with Hunterbrook, Citrini Research and Novus Capital, detailed a de novo protein design campaign that successfully generated binders against scorpion toxins, a strategy diverging from traditional antivenom production.
The team, led by Amir Shanehsazzadeh, used Claude Science to execute the design process, resulting in proteins created from scratch rather than relying on pre-existing antibodies or fragments. Researchers then experimentally characterized these proteins, confirming their ability to bind to scorpion toxins.
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