Cyclization strategies of meditopes: affinity and diffraction studies of meditope-Fab complexes.

ABSTRACT: Recently, a unique binding site for a cyclic 12-residue peptide was discovered within a cavity formed by the light and heavy chains of the cetuximab Fab domain. In order to better understand the interactions that drive this unique complex, a number of variants including the residues within the meditope peptide and the antibody, as well as the cyclization region of the meditope peptide, were created. Here, multiple crystal structures of meditope peptides incorporating different cyclization strategies bound to the central cavity of the cetuximab Fab domain are presented. The affinity of each cyclic derivative for the Fab was determined by surface plasmon resonance and correlated to structural differences. Overall, it was observed that the disulfide bond used to cyclize the peptide favorably

SUBMITTER: Bzymek KP 

PROVIDER: S-EPMC4909242 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature