Predicting Antibody Affinity Changes upon Mutation Based on Unbound Protein Structures.

ABSTRACT: Antibodies are key proteins in the immune system that can reversibly and non-covalently bind specifically to their corresponding antigens, forming antigen-antibody complexes. They play a crucial role in recognizing foreign or self-antigens during the adaptive immune response. Monoclonal antibodies have emerged as a promising class of biological macromolecule therapeutics with broad market prospects. In the process of antibody drug development, a key engineering challenge is to improve the affinity of candidate antibodies, without experimentally resolved structures of the antigen-antibody complexes as input for computer-aided predictive methods. In this work, we present an approach for predicting the effect of residue mutations on antibody affinity without the structures of the antigen-anti

SUBMITTER: Chen Z 

PROVIDER: S-EPMC11818220 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature