Arginine mutations in antibody complementarity-determining regions display context-dependent affinity/specificity trade-offs.

ABSTRACT: Antibodies commonly accumulate charged mutations in their complementarity-determining regions (CDRs) during affinity maturation to enhance electrostatic interactions. However, charged mutations can mediate non-specific interactions, and it is unclear to what extent CDRs can accumulate charged residues to increase antibody affinity without compromising specificity. This is especially concerning for positively charged CDR mutations that are linked to antibody polyspecificity. To better understand antibody affinity/specificity trade-offs, we have selected single-chain antibody fragments specific for the negatively charged and hydrophobic Alzheimer's amyloid β peptide using weak and stringent selections for antibody specificity. Antibody variants isolated using weak selections for specificity

SUBMITTER: Tiller KE 

PROVIDER: S-EPMC5633126 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature