Role of the Trp-disulfide Triads in the UV Light Induced Degradation of a Monoclonal Antibody scFv.
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Date
2014-09
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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.