A single-domain antibody library based on a stability-engineered human VH3 scaffold.

ABSTRACT: Using conventional immunoglobulin G (IgG) molecules as therapeutic agents presents several well-known disadvantages owing to their large size and structural complexity, negatively impacting development and production efficiency. Single-domain antibodies (sdAbs) are the smallest functional antibody format (~ 15 kDa) and represent a viable alternative to IgG in many applications. However, unlike natural single-domain antibodies, such as camelid V_HH, the variable domains of conventional antibodies show poor physicochemical properties when expressed as sdAbs. This report identified stable sdAb variants of human VH3-23 from a framework region 2-randomized human VH library by phage display selection under thermal challenge. Synthetic complementarity determining region diversity was in

SUBMITTER: Lee NJ 

PROVIDER: S-EPMC11291719 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature