Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/89273
Title: Selective modification of alkyne-linked peptides and proteins by cyclometalated gold(III) (C^N) complex-mediated alkynylation
Authors: Ko, HM 
Deng, JR 
Cui, JF 
Kung, KKY 
Leung, YC 
Wong, MK 
Issue Date: 1-Apr-2020
Source: Bioorganic & medicinal chemistry, 1 Apr. 2020, v. 28, no. 7, 115375
Abstract: Alkyne is a useful functionality incorporated in proteins for site-selective bioconjugation reactions. Although effective bioconjugation reactions such as copper(I)-catalyzed and/or copper-free 1,3-dipolar cycloadditions of alkynes and azides are the most common approaches, the development of new alkyne-based bioconjugation reactions is still an ongoing interest in chemical biology. In this work, a new approach has been developed for selective modification of alkyne-linked peptides and proteins through the formation of arylacetylenes by a cross-coupling reaction of 6-membered ring cyclometalated gold(III) (C^N) complexes (HC^N = 2-arylpyridines) with terminal alkynes. Screening of the reaction conditions with a series of cyclometalated gold(III) complexes with phenylacetylene gave an excellent yield (up to 82%) by conducting the reaction in slightly alkaline aqueous conditions. The reaction scope was expanded to various alkynes, including alkyne-linked peptides to achieve up to >99% conversion. Using fluorescent dansyl (1l) and BODIPY (1m)-linked gold(III) complexes, alkyne-linked lysozyme has been selectively modified.
Keywords: Alkynylation
Bioconjugation reaction
Gold complexes
Protein modification
Publisher: Pergamon Press
Journal: Bioorganic & medicinal chemistry 
ISSN: 0968-0896
EISSN: 1464-3391
DOI: 10.1016/j.bmc.2020.115375
Appears in Collections:Journal/Magazine Article

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