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Indexed by:期刊论文

Date of Publication:2016-10-01

Journal:BIOCONJUGATE CHEMISTRY

Included Journals:SCIE、PubMed、Scopus

Volume:27

Issue:10

Page Number:2266-2270

ISSN No.:1043-1802

Abstract:A strategy for photoinduced covalent immobilization of proteins on phenol-functionalized surfaces is described. Under visible light irradiation, the reaction can be completed within seconds at ambient temperature, with high yields in aqueous solution of physiological conditions. Protein immobilization is based on a ruthenium-catalyzed radical cross-linking reaction between proteins and phenol-modified surfaces, and the process has proven mild enough for lipase, Staphylococcus aureus protein A, and streptavidin to preserve their bioactivity. This strategy was successfully applied to antibody immobilization on different material platforms, including agarose beads, cellulose membranes, and glass wafers, thus providing a generic procedure for rapid biomodification of surfaces.