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Article: Modification of N-terminal α-amino groups of peptides and proteins using ketenes

TitleModification of N-terminal α-amino groups of peptides and proteins using ketenes
Authors
Issue Date2012
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
Citation
Journal Of The American Chemical Society, 2012, v. 134 n. 5, p. 2589-2598 How to Cite?
AbstractA method of highly selective N-terminal modification of proteins as well as peptides by an isolated ketene was developed. Modification of a library of unprotected peptides XSKFR (X varies over 20 natural amino acids) by an alkyne-functionalized ketene (1) at room temperature at pH 6.3 resulted in excellent N-terminal selectivity (modified α-amino group/modified ε-amino group = >99:1) for 13 out of the 20 peptides and moderate-to-high N-terminal selectivity (4:1 to 48:1) for 6 of the 7 remaining peptides. Using an alkyne-functionalized N-hydroxysuccinimide (NHS) ester (2) instead of 1, the modification of peptides XSKFR gave internal lysine-modified peptides for 5 out of the 20 peptides and moderate-to-low N-terminal selectivity (5:1 to 1:4) for 13 out of the 20 peptides. Proteins including insulin, lysozyme, RNaseA, and a therapeutic protein BCArg were selectively N-terminally modified at room temperature using ketene 1, in contrast to the formation of significant or major amounts of di-, tri-, or tetra-modified proteins in the modification by NHS ester 2. The 1-modified proteins were further functionalized by a dansyl azide compound through click chemistry without the need for prior treatment. © 2012 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/159410
ISSN
2015 Impact Factor: 13.038
2015 SCImago Journal Rankings: 7.123
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChan, AOYen_HK
dc.contributor.authorHo, CMen_HK
dc.contributor.authorChong, HCen_HK
dc.contributor.authorLeung, YCen_HK
dc.contributor.authorHuang, JSen_HK
dc.contributor.authorWong, MKen_HK
dc.contributor.authorChe, CMen_HK
dc.date.accessioned2012-08-16T05:49:09Z-
dc.date.available2012-08-16T05:49:09Z-
dc.date.issued2012en_HK
dc.identifier.citationJournal Of The American Chemical Society, 2012, v. 134 n. 5, p. 2589-2598en_HK
dc.identifier.issn0002-7863en_HK
dc.identifier.urihttp://hdl.handle.net/10722/159410-
dc.description.abstractA method of highly selective N-terminal modification of proteins as well as peptides by an isolated ketene was developed. Modification of a library of unprotected peptides XSKFR (X varies over 20 natural amino acids) by an alkyne-functionalized ketene (1) at room temperature at pH 6.3 resulted in excellent N-terminal selectivity (modified α-amino group/modified ε-amino group = >99:1) for 13 out of the 20 peptides and moderate-to-high N-terminal selectivity (4:1 to 48:1) for 6 of the 7 remaining peptides. Using an alkyne-functionalized N-hydroxysuccinimide (NHS) ester (2) instead of 1, the modification of peptides XSKFR gave internal lysine-modified peptides for 5 out of the 20 peptides and moderate-to-low N-terminal selectivity (5:1 to 1:4) for 13 out of the 20 peptides. Proteins including insulin, lysozyme, RNaseA, and a therapeutic protein BCArg were selectively N-terminally modified at room temperature using ketene 1, in contrast to the formation of significant or major amounts of di-, tri-, or tetra-modified proteins in the modification by NHS ester 2. The 1-modified proteins were further functionalized by a dansyl azide compound through click chemistry without the need for prior treatment. © 2012 American Chemical Society.en_HK
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.htmlen_HK
dc.relation.ispartofJournal of the American Chemical Societyen_HK
dc.subject.meshEthylenes - chemical synthesis - chemistryen_HK
dc.subject.meshKetones - chemical synthesis - chemistryen_HK
dc.subject.meshModels, Molecularen_HK
dc.subject.meshMolecular Structureen_HK
dc.subject.meshPeptides - chemistryen_HK
dc.subject.meshProteins - chemistryen_HK
dc.subject.meshStereoisomerismen_HK
dc.titleModification of N-terminal α-amino groups of peptides and proteins using ketenesen_HK
dc.typeArticleen_HK
dc.identifier.emailHo, CM: rickyho@hkucc.hku.hken_HK
dc.identifier.emailChe, CM: cmche@hku.hken_HK
dc.identifier.authorityHo, CM=rp00705en_HK
dc.identifier.authorityChe, CM=rp00670en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/ja208009ren_HK
dc.identifier.pmid22288779-
dc.identifier.scopuseid_2-s2.0-84863012427en_HK
dc.identifier.hkuros205421en_US
dc.identifier.hkuros204505-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84863012427&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume134en_HK
dc.identifier.issue5en_HK
dc.identifier.spage2589en_HK
dc.identifier.epage2598en_HK
dc.identifier.isiWOS:000300460600032-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridChan, AOY=55268421200en_HK
dc.identifier.scopusauthoridHo, CM=12807243800en_HK
dc.identifier.scopusauthoridChong, HC=36804350200en_HK
dc.identifier.scopusauthoridLeung, YC=35074432700en_HK
dc.identifier.scopusauthoridHuang, JS=54964622200en_HK
dc.identifier.scopusauthoridWong, MK=7403908449en_HK
dc.identifier.scopusauthoridChe, CM=7102442791en_HK

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