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dc.contributorDepartment of Applied Biology and Chemical Technology-
dc.creatorDeng, JR-
dc.creatorChung, SF-
dc.creatorLeung, ASL-
dc.creatorYip, WM-
dc.creatorYang, B-
dc.creatorChoi, MC-
dc.creatorCui, JF-
dc.creatorKung, KKY-
dc.creatorZhang, Z-
dc.creatorLo, KW-
dc.creatorLeung, YC-
dc.creatorWong, MK-
dc.publisherNature Publishing Groupen_US
dc.rightsOpen Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing,adaptation, distribution and reproduction in any medium or format, as long as you giveappropriate credit to the original author(s) and the source, provide a link to the CreativeCommons license, and indicate if changes were made. The images or other third partymaterial in this article are included in the article’s Creative Commons license, unlessindicated otherwise in a credit line to the material. If material is not included in thearticle’s Creative Commons license and your intended use is not permitted by statutoryregulation or exceeds the permitted use, you will need to obtain permission directly fromthe copyright holder. To view a copy of this license, visit
dc.rights© The Author(s) 2019en_US
dc.rightsThe following publication Deng, J. R., Chung, S. F., Leung, A. S. L., Yip, W. M., Yang, B., Choi, M. C., . . . Wong, M. K. (2019). Chemoselective and photocleavable cysteine modification of peptides and proteins using isoxazoliniums. Communications Chemistry, 2, 93, 1-10 is available at
dc.titleChemoselective and photocleavable cysteine modification of peptides and proteins using isoxazoliniumsen_US
dc.typeJournal/Magazine Articleen_US
dcterms.abstractIt is of ongoing interest to develop new approaches for efficient and selective modification of cysteine residues on biomolecules. Here we present a comprehensive study on a newly developed isoxazolinium-mediated cysteine modification of peptides and proteins. Using a stoichiometric amount of isoxazolinium reagents generated in situ from a catalytic amount of silver salts, cysteine-containing peptides can be efficiently modified to afford products in nearly complete conversions. With the optimized conditions, free cysteine containing proteins HSA and BSA, as well as a site-directed mutated therapeutic protein (BCArg) can be efficiently and selectively labelled using small amounts of the isoxazolinium reagents. We find that the phenylacyl thioether linkage bearing an alkyne moiety can be rapidly cleaved under irradiation of UV-A light, giving the formation of a thioaldehyde moiety, which can be converted back to cysteine by reduction.-
dcterms.bibliographicCitationCommunications chemistry, 9 Aug. 2019, v. 2, 93, p. 1-10-
dcterms.isPartOfCommunications chemistry-
dc.description.validate201909 bcrc-
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