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Title: Site-specific dual functionalization of cysteine residue in peptides and proteins with 2-azidoacrylates
Authors: Ariyasu, Shinya
Hayashi, Hirohito
Xing, Bengang
Chiba, Shunsuke
Keywords: Science::Chemistry
Issue Date: 2017
Source: Ariyasu, S., Hayashi, H., Xing, B. & Chiba, S. (2017). Site-specific dual functionalization of cysteine residue in peptides and proteins with 2-azidoacrylates. Bioconjugate Chemistry, 28(4), 897-902.
Project: RG2/15 
Journal: Bioconjugate Chemistry 
Abstract: Herein, we report use of 2-azidoacrylates to perform site-specific dual functionalization of the cysteine residue of peptides and bovine serum albumin (BSA), a native protein containing one free cysteine residue. The sulfhydryl group of the cysteine residue could be conjugated with 2-azidoacrylates bearing various functionalities, such as fluorescent dyes under physiological aqueous buffer conditions, to afford peptide and protein conjugates anchoring an azide moiety. Successive azide-alkyne cycloaddition enables installation of the second functionality, thus affording dual-functionalized peptide- and protein-based materials.
ISSN: 1043-1802
DOI: 10.1021/acs.bioconjchem.7b00024
Schools: School of Physical and Mathematical Sciences 
Rights: This document is the Accepted Manuscript version of a Published Work that appeared in final form in Bioconjugate Chemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SPMS Journal Articles

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