Cross-linking disulfide bonds govern solution structures of diabodies.

ABSTRACT: In the last years, antibodies have emerged as a promising new class of therapeutics, due to their combination of high specificity with long serum half-life and low risk of side-effects. Diabodies are a popular novel antibody format, consisting of two F_v domains connected with short linkers. Like IgG antibodies, they simultaneously bind two target proteins. However, they offer altered properties, given their smaller size and higher rigidity. In this study, we conducted the-to our knowledge-first molecular dynamics (MD) simulations of diabodies and find a surprisingly high conformational flexibility in the relative orientation of the two F_v domains. We observe rigidifying effects through the introduction of disulfide bonds in the F_v -F_v interface a

SUBMITTER: Math BA 

PROVIDER: S-EPMC10952579 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature