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Article: Enabling N-to-C Ser/Thr Ligation for Convergent Protein Synthesis via Combining Chemical Ligation Approaches

TitleEnabling N-to-C Ser/Thr Ligation for Convergent Protein Synthesis via Combining Chemical Ligation Approaches
Authors
Issue Date2016
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, 2016, v. 138 n. 33, p. 10477-10484 How to Cite?
AbstractIn this article, Ser/Thr ligationon/off has been realized to enable N-to-C successive peptide ligations using a salicylaldehyde semicarbazone (SALoff) group by in situ activation with pyruvic acid of the peptide SALoff ester into the peptide salicylaldehyde (SALon) ester. In addition, a peptide with a C-terminal thioester and N-terminal Ser or Thr as the middle peptide segment can undergo one-pot Ser/Thr ligation and native chemical ligation in the N-to-C direction. The utility of this combined ligation strategy in the N-to-C direction has been showcased through the convergent assembly of a human cytokine protein sequence, GlcNAcylated interleukin-25.
Persistent Identifierhttp://hdl.handle.net/10722/234029
ISSN
2019 Impact Factor: 14.612
2015 SCImago Journal Rankings: 7.123
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLee, CL-
dc.contributor.authorLiu, H-
dc.contributor.authorWong, CTT-
dc.contributor.authorChow, HY-
dc.contributor.authorLi, X-
dc.date.accessioned2016-10-14T06:58:35Z-
dc.date.available2016-10-14T06:58:35Z-
dc.date.issued2016-
dc.identifier.citationJournal of the American Chemical Society, 2016, v. 138 n. 33, p. 10477-10484-
dc.identifier.issn0002-7863-
dc.identifier.urihttp://hdl.handle.net/10722/234029-
dc.description.abstractIn this article, Ser/Thr ligationon/off has been realized to enable N-to-C successive peptide ligations using a salicylaldehyde semicarbazone (SALoff) group by in situ activation with pyruvic acid of the peptide SALoff ester into the peptide salicylaldehyde (SALon) ester. In addition, a peptide with a C-terminal thioester and N-terminal Ser or Thr as the middle peptide segment can undergo one-pot Ser/Thr ligation and native chemical ligation in the N-to-C direction. The utility of this combined ligation strategy in the N-to-C direction has been showcased through the convergent assembly of a human cytokine protein sequence, GlcNAcylated interleukin-25.-
dc.languageeng-
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html-
dc.relation.ispartofJournal of the American Chemical Society-
dc.titleEnabling N-to-C Ser/Thr Ligation for Convergent Protein Synthesis via Combining Chemical Ligation Approaches-
dc.typeArticle-
dc.identifier.emailLiu, H: liuhan@hku.hk-
dc.identifier.emailWong, CTT: cttwong@HKUCC-COM.hku.hk-
dc.identifier.emailLi, X: xuechenl@hku.hk-
dc.identifier.authorityLiu, H=rp02748-
dc.identifier.authorityLi, X=rp00742-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/jacs.6b04238-
dc.identifier.pmid27479006-
dc.identifier.scopuseid_2-s2.0-84983591523-
dc.identifier.hkuros267610-
dc.identifier.volume138-
dc.identifier.issue33-
dc.identifier.spage10477-
dc.identifier.epage10484-
dc.identifier.isiWOS:000382181900021-
dc.publisher.placeUnited States-
dc.identifier.issnl0002-7863-

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