Role of the Trp-disulfide Triads in the UV Light Induced Degradation of a Monoclonal Antibody scFv.

Abstract
Proteins are targets for photodegradation due to absorption of incident light by endogenous chromophores, e.g aromatic side chains. In this work we study the role of Trp-disulfide triads in the light induced loss of immunoglobulin activity. Study Design: We investigated a single chain variable fragment (scFv) of the Trp-disulfide triad containing monoclonal antibody 82D6A3. The scFv binds to von Willebrand factor (VWF) and upon illumination with near UV-B-light the scFv partially loses its binding capacity to VWF. In order to relate this observed degeneration to the specific Trp-disulfide triads, we mutated W35(VL) and W36(VH) which are in direct contact with the disulfide
Description
Keywords
Immunoglobulin, Trp-Phe mutants, tryptophan fluorescence, disulfide bonds, photolysis, aggregation, scFv
Citation
Illyés Eszter, Staelens Stephanie, Vanhooren Ann, Deckmyn Hans, Hanssens Ignace, Majer Zsuzsa. Role of the Trp-disulfide Triads in the UV Light Induced Degradation of a Monoclonal Antibody scFv. International Journal of Biochemistry Research & Review 2014 Sept-Oct ; 4 (5) : 367-385.