Delicate balance among thermal stability, binding affinity, and conformational space explored by single-domain V_HH antibodies.

ABSTRACT: The high binding affinities and specificities of antibodies have led to their use as drugs and biosensors. Single-domain V_HH antibodies exhibit high specificity and affinity but have higher stability and solubility than conventional antibodies as they are single-domain proteins. In this work, based on physicochemical measurements and molecular dynamics (MD) simulations, we have gained insight that will facilitate rational design of single-chain V_HH antibodies. We first assessed two homologous V_HH antibodies by differential scanning calorimetry (DSC); one had a high (64.8 °C) and the other a low (58.6 °C) melting temperature. We then generated a series of the variants of the low stability antibody and analyzed their thermal stabilities by DSC and characteriz

SUBMITTER: Ikeuchi E 

PROVIDER: S-EPMC8523659 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature