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Biology subjects

Kantorow, J.

Publications and source records attributed to Kantorow, J..

3 recordsLinked to original sources

F.A.D.E. (Fully Agentic Drug Engine): A Conversational AI Platform for Drug Discovery

Drug discovery remains one of the costliest and most time-intensive endeavors in the pharmaceutical pipeline, with average development costs exceeding $2.3 billion per drug, timelines spanning more than a decade, and attrition rates above 90% in clinical trials. While computational methods have expanded the searchable chemical space, current pipelines remain fragmented and largely inaccessible to researchers without deep interdisciplinary expertise. Here we present F.A.D.E. (Fully Agentic Drug Engine), a multi-agent, open-source platform that converts natural language queries into potential drug candidates, substantially lowering the expertise barrier to advanced computational drug discovery. F.A.D.E. employs a three-branch hierarchical architecture that adapts to the level of available structural data for any protein target, integrating structure prediction, binding pocket detection, equivariant diffusion-based de novo ligand generation, and binding affinity estimation into a single automated pipeline. We validate F.A.D.E. on two structurally distinct targets: the epidermal growth factor receptor kinase domain (EGFR), a well-established oncology target, and cellular retinol-binding protein 1 (CRBP1), a lipid-binding protein involved in retinoid metabolism. For EGFR, our generated candidates achieved QED scores of 0.85 compared to 0.46 for the co-crystallised reference ligand, demonstrating marked improvement in predicted drug-likeness. Results across both targets confirm that F.A.D.E. can reliably generate chemically tractable, drug-like hit compounds across diverse protein classes from simple natural language input.

biophysics↗

Interpretable Antibody-Antigen Structural Interface Prediction via Adaptive Graph Learning and Cyclic Transfer

Experimental structural methods can identify antibody-antigen interfaces with high precision, but they remain time-consuming and resource-intensive, limiting their application across the rapidly expanding space of antibody and antigen sequences. Computational models capable of predicting these interfaces could therefore accelerate antibody discovery and provide insight into the principles governing immune recognition. However, this problem remains challenging due to limited structural datasets, severe class imbalance, and the complex, non-local nature of biomolecular interactions. Here we present VASCIF (Variable-domain Antibody-antigen Structural Complex Interface Finder), a structure-aware framework built on a Masked Graph Attention (MGA) architecture that represents protein complexes as residue graphs and captures long-range structural dependencies through attention-based message passing. The framework is straightforward to implement and enables efficient inference, allowing substantially faster predictions than other existing structure-based approaches. Evaluated on curated structural complexes across multiple benchmark datasets using rigorous cross-validation, VASCIF achieves state-of-the-art performance for residue-level interface prediction. Interpretability analyses reveal that the model recovers biophysically meaningful interaction patterns consistent with known principles of antibody recognition, and redefining interfaces using larger residue distance thresholds ([~]10 [A]) significantly improves predictive performance. Together, VASCIF provides a practical predictive framework and new insights into antibody-antigen molecular recognition.

bioinformatics↗

Structural and immunological characterization of the H3 influenza hemagglutinin during antigenic drift

The quest for a universal influenza vaccine holds great promise for mitigating the global burden of influenza-related morbidity and mortality. However, challenges persist in identifying conserved epitopes capable of inducing protection. In this study, we explore the influence of glycan evolution on H3 hemagglutinin from 1968 to present day and its impacts on antigenicity and immunogenicity. We observe that the appearance of potential N-linked glycosylation sites in Sing/16 hemagglutinin head domain reduces the binding of broadly neutralizing antibodies and shifts the polyclonal immune response upon vaccination to target the stem. Furthermore, structural characterization of HK/68 and Sing/16 by cryo-electron microscopy shows that while HK/68 is resistant to enzymatic deglycosylation, removal of glycans destabilizes the hyperglycosylated head and membrane-proximal region in Sing/16. These insights expand our understanding of glycans beyond their role in protein folding and highlight the interplay among glycan integration and immune recognition to design a universal influenza vaccine.

immunology↗