Structure of the Anti-C60 Fullerene Antibody Fab Fragment: Structural Determinants of Fullerene Binding.

ABSTRACT: The structure of the anti-C₆₀ fullerene antibody Fab fragment (FabC₆₀) was solved by X-ray crystallography. The computer-aided docking of C₆₀ into the antigen-binding pocket of FabC₆₀ showed that binding of C₆₀ to FabC₆₀ is governed by the enthalpy and entropy; namely, by π-π stacking interactions with aromatic residues of the antigen-binding site and reduction of the solvent-accessible area of the hydrophobic surface of C₆₀. A fragment of the mobile CDR H3 loop located on the surface of FabC₆₀ interferes with C₆₀ binding in the antigen-binding site, thereby resulting in low antibody affinity for C₆₀. The structure of apo-FabC₆₀ has been deposited with pdbid 6H3H.

SUBMITTER: Osipov EM 

PROVIDER: S-EPMC6475864 | biostudies-literature | 2019 Jan-Mar

REPOSITORIES: biostudies-literature