Atomic-level thermodynamics analysis of the binding free energy of SARS-CoV-2 neutralizing antibodies.

ABSTRACT: Understanding how protein-protein binding affinity is determined from molecular interactions at the interface is essential in developing protein therapeutics such as antibodies, but this has not yet been fully achieved. Among the major difficulties are the facts that it is generally difficult to decompose thermodynamic quantities into contributions from individual molecular interactions and that the solvent effect-dehydration penalty-must also be taken into consideration for every contact formation at the binding interface. Here, we present an atomic-level thermodynamics analysis that overcomes these difficulties and illustrate its utility through application to SARS-CoV-2 neutralizing antibodies. Our analysis is based on the direct interaction energy computed from simulated antibody-prote

SUBMITTER: Lee J 

PROVIDER: S-EPMC9880660 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature