arXiv:2607. 05846v1 Announce Type: cross Abstract: Accurate ranking of antibody candidates according to their binding affinity is essential for therapeutic antibody discovery.
Accurate ranking of antibody candidates according to their binding affinity is essential for therapeutic antibody discovery. However, existing methods treat affinity comparisons independently and ignore the contextual information encoded in other labeled comparisons, limiting their ability to capture antigen-specific binding landscapes.
arXiv:2607. 16263v1 Announce Type: new Abstract: Antibody expression ranking is a critical task in antibody design, yet its modelling is severely hindered by the scarcity of labeled experimental data.
arXiv:2606. 04154v1 Announce Type: cross Abstract: Antibodies neutralize foreign antigens by binding to specific surface regions called epitopes.
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:2608.30175v1 Announce Type: new Abstract: Peptide-protein affinity models are often evaluated with a single data split, obscuring whether they interpolate among measurements for observed target...
arXiv:2607. 20057v1 Announce Type: cross Abstract: Antibodies are essential proteins that play a central role in immune recognition by binding specific antigen molecules.
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.
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. 18703v1 Announce Type: new Abstract: Pretrained biological language models expose per-token probability distributions through masked-token prediction, providing the likelihood interface central to sequence design, variant scoring, and mechanistic interpretation.
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.
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.