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Article: Traceless and Chemoselective Amine Bioconjugation via Phthalimidine Formation in Native Protein Modification

TitleTraceless and Chemoselective Amine Bioconjugation via Phthalimidine Formation in Native Protein Modification
Authors
Issue Date2016
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/orlef7/index.html
Citation
Organic Letters, 2016, v. 18, p. 2600-2603 How to Cite?
Abstractortho-Phthalaldehyde (OPA) and its derivatives are found to react chemoselectively with amino groups on peptides and proteins rapidly and tracelessly under the physiological condition via formation of phthalimidines, which provides a novel and promising approach when performing bioconjugation on native proteins. The notable advantages of this method over the existing native protein lysine-labeling approaches include a traceless process, a self-reacting, specific and fast reaction, ease of operation, and the ability to use nonhydrolyzable reagents. Its applications have been effectively demonstrated including conjugation of peptides and proteins, and generation of an active PEGlyated l-asparaginase.
Persistent Identifierhttp://hdl.handle.net/10722/231683
ISSN
2023 Impact Factor: 4.9
2023 SCImago Journal Rankings: 1.245

 

DC FieldValueLanguage
dc.contributor.authorTUNG, CL-
dc.contributor.authorWong, CTT-
dc.contributor.authorFung, EYM-
dc.contributor.authorLi, XC-
dc.date.accessioned2016-09-20T05:24:50Z-
dc.date.available2016-09-20T05:24:50Z-
dc.date.issued2016-
dc.identifier.citationOrganic Letters, 2016, v. 18, p. 2600-2603-
dc.identifier.issn1523-7060-
dc.identifier.urihttp://hdl.handle.net/10722/231683-
dc.description.abstractortho-Phthalaldehyde (OPA) and its derivatives are found to react chemoselectively with amino groups on peptides and proteins rapidly and tracelessly under the physiological condition via formation of phthalimidines, which provides a novel and promising approach when performing bioconjugation on native proteins. The notable advantages of this method over the existing native protein lysine-labeling approaches include a traceless process, a self-reacting, specific and fast reaction, ease of operation, and the ability to use nonhydrolyzable reagents. Its applications have been effectively demonstrated including conjugation of peptides and proteins, and generation of an active PEGlyated l-asparaginase.-
dc.languageeng-
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/orlef7/index.html-
dc.relation.ispartofOrganic Letters-
dc.titleTraceless and Chemoselective Amine Bioconjugation via Phthalimidine Formation in Native Protein Modification-
dc.typeArticle-
dc.identifier.emailWong, CTT: cttwong@HKUCC-COM.hku.hk-
dc.identifier.emailFung, EYM: eva.fungym@hku.hk-
dc.identifier.emailLi, XC: xuechenl@hku.hk-
dc.identifier.authorityFung, EYM=rp01986-
dc.identifier.authorityLi, XC=rp00742-
dc.identifier.doi10.1021/acs.orglett.6b00983.-
dc.identifier.hkuros265984-
dc.identifier.volume18-
dc.identifier.spage2600-
dc.identifier.epage2603-
dc.publisher.placeUnited States-
dc.identifier.issnl1523-7052-

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