arXiv:2606. 04154v1 Announce Type: cross Abstract: Antibodies neutralize foreign antigens by binding to specific surface regions called epitopes.
arXiv:2605. 21610v2 Announce Type: replace Abstract: Antibody design methods condition on antigen structure to generate complementarity-determining regions (CDR), yet a systematic evaluation of baseline methods reveals that they largely ignore the antigen input.
DuaDeep-SeqAffinity is a sequence-only deep learning framework that predicts antibody–antigen binding affinity directly from primary amino acid sequences, eliminating the need for resolved 3D structures. The model processes the antigen and the antibody heavy and light chains as three independent streams, each embedded with a frozen ESM‑2 protein language model and passed through parallel Transformer and CNN branches before late fusion. On a sequence‑disjoint split of the AbRank benchmark, it achieves a Pearson correlation of 0.683, an R² of 0.460, and a pairwise ranking AUC of 0.895, outperforming single‑branch ablations and showing attention to CDR loops and epitope residues.
arXiv:2603. 13431v3 Announce Type: replace-cross Abstract: Computational antibody design has seen rapid methodological progress, with dozens of deep generative methods proposed in the past three years, yet the field lacks a standardized benchmark for fair comparison and model development.
The paper introduces Explainability from Training (EFT), a model‑agnostic method that tracks how deep learning models learn and organize evidence during training. EFT is applied to four leading T cell receptor‑epitope prediction models, revealing distinct learning trajectories for CNNs and transformers, conflicts between TCR alpha and beta chain evidence, and differences in feature preferences when using real versus predicted structural data. The authors also present a new benchmark, TCR‑XAI2, comprising 388 experimentally resolved TCR‑epitope structures and several predicted models to evaluate these insights.
arXiv:2606. 28659v1 Announce Type: cross Abstract: High-fidelity molecular docking simulations can produce biologically relevant estimates of epitope-receptor binding affinity but are computationally expensive and therefore limit the number of candidates that can be screened for vaccine design.
arXiv:2609.00518v1 Announce Type: new Abstract: Antibody-specific language models pretrained via masked language modeling (MLM) learn representations that are critical for downstream sequence design...
arXiv:2607. 20057v1 Announce Type: cross Abstract: Antibodies are essential proteins that play a central role in immune recognition by binding specific antigen molecules.
arXiv:2605. 21600v2 Announce Type: replace Abstract: Computational antibody CDR design methods condition on antigen structure to generate binding loops.
Antibodies are essential proteins that play a central role in immune recognition by binding specific antigen molecules. Although recent protein language models have enabled progress in single-chain protein modeling and generation, they often fall short in antigen-specific antibody design, where effective modeling requires explicit pairing between antibody and antigen, particularly at the epitope level.
arXiv:2602. 17330v5 Announce Type: replace-cross Abstract: Comparative analysis of adaptive immune repertoires at population scale is hampered by two practical bottlenecks: the near-quadratic cost of pairwise affinity evaluations and dataset imbalances that obscure clinically important minority clonotypes.
arXiv:2606. 23830v1 Announce Type: cross Abstract: Molecular surfaces encode the geometric and physicochemical patterns that determine antibody-antigen recognition, central to epitope prediction.
arXiv:2607. 05846v1 Announce Type: cross Abstract: Accurate ranking of antibody candidates according to their binding affinity is essential for therapeutic antibody discovery.