CDR loop interactions can determine heavy and light chain pairing preferences in bispecific antibodies.

ABSTRACT: As the current biotherapeutic market is dominated by antibodies, the design of different antibody formats, like bispecific antibodies, is critical to the advancement of the field. In contrast to monovalent antibodies, which consist of two identical antigen-binding sites, bispecific antibodies can target two different epitopes by containing two different antigen-binding sites. Thus, the rise of new formats as successful therapeutics has reignited the interest in advancing and facilitating the efficient production of bispecific antibodies. Here, we investigate the influence of point mutations in the antigen-binding site, the paratope, on heavy and light chain pairing preferences by using molecular dynamics simulations. In agreement with experiments, we find that specific residues in the anti

SUBMITTER: Fernandez-Quintero ML 

PROVIDER: S-EPMC8803122 | biostudies-literature | 2022 Jan-Dec

REPOSITORIES: biostudies-literature