摘要

We performed metadynamics molecular dynamics simulations to reveal mechanism of antigen-dependent fluorescence response observed for site-specifically fluorescent-labeled single-chain antibody against c-Myc peptide antigen. We found that V-H and V-L bind with each other only when the antigen exists and that the fluorophore labeled at the N-terminus of V-H interacts with Trp103 most stably. These results support the mechanism proposed from previous experiments: In the absence of antigen, Trp residues are partially exposed at the interface of V-H and quench the fluorophore. In the presence of antigen, the Trp residues are buried between V-H and V-L, and the quenching is eliminated.

  • 出版日期2018-4-16