Ontology highlight
ABSTRACT:
SUBMITTER: Pomarici ND
PROVIDER: S-EPMC9741699 | biostudies-literature | 2022 Feb
REPOSITORIES: biostudies-literature
Pomarici Nancy D ND Fernández-Quintero Monica L ML Quoika Patrick K PK Waibl Franz F Bujotzek Alexander A Georges Guy G Liedl Klaus R KR
Protein engineering, design & selection : PEDS 20220201
A new format of therapeutic proteins is bispecific antibodies, in which two different heavy chains heterodimerize to obtain two different binding sites. Therefore, it is crucial to understand and optimize the third constant domain (CH3-CH3) interface to favor heterodimerization over homodimerization, and to preserve the physicochemical properties, as thermal stability. Here, we use molecular dynamics simulations to investigate the dissociation process of 19 CH3-CH3 crystal structures that differ ...[more]