Effective binding to protein antigens by antibodies from antibody libraries designed with enhanced protein recognition propensities.

ABSTRACT: Antibodies provide immune protection by recognizing antigens of diverse chemical properties, but elucidating the amino acid sequence-function relationships underlying the specificity and affinity of antibody-antigen interactions remains challenging. We designed and constructed phage-displayed synthetic antibody libraries with enriched protein antigen-recognition propensities calculated with machine learning predictors, which indicated that the designed single-chain variable fragment variants were encoded with enhanced distributions of complementarity-determining region (CDR) hot spot residues with high protein antigen recognition propensities in comparison with those in the human antibody germline sequences. Antibodies derived directly from the synthetic antibody libraries, without affinit

SUBMITTER: Jian JW 

PROVIDER: S-EPMC6380391 | biostudies-literature | 2019 Feb/Mar

REPOSITORIES: biostudies-literature