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:2606. 04154v1 Announce Type: cross Abstract: Antibodies neutralize foreign antigens by binding to specific surface regions called epitopes.
By Mansoor Ahmed, Huirong Chai, Haoxin Wang, Hemanth Venkateswara, Murray Patterson
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.
By Mansoor Ahmed, Nadeem Taj, Imdad Ullah Khan, Hemanth Venkateswara, Murray Patterson
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.
By Mansoor Ahmed, Murray Patterson
arXiv:2605. 21600v2 Announce Type: replace Abstract: Computational antibody CDR design methods condition on antigen structure to generate binding loops.
By Mansoor Ahmed, Spencer VonBank, Nadeem Taj, Sujin Lee, Naila Jan, Murray Patterson
arXiv:2607. 05846v1 Announce Type: cross Abstract: Accurate ranking of antibody candidates according to their binding affinity is essential for therapeutic antibody discovery.
By Zhiyuan Chen, Jing Hu, Junzhe Wang, Yueyang Huang, Xinyi Yang, Zhaoyang Wang, Feng Zhu