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Article: Cysteine/Penicillamine Ligation Independent of Terminal Steric Demands for Chemical Protein Synthesis

TitleCysteine/Penicillamine Ligation Independent of Terminal Steric Demands for Chemical Protein Synthesis
Authors
Keywordschemical ligation
chemical protein synthesis
peptide desulfurization
peptides
proteins
Issue Date2020
PublisherWiley - V C H Verlag GmbH & Co. KGaA. The Journal's web site is located at http://www.angewandte.de
Citation
Angewandte Chemie, 2020, v. 132 n. 31, p. 12841-12845 How to Cite?
AbstractThe chemical ligation of two unprotected peptides to generate a natural peptidic linkage specifically at the C‐ and N‐termini is a desirable goal in chemical protein synthesis but is challenging because it demands high reactivity and selectivity (chemo‐, regio‐, and stereoselectivity). We report an operationally simple and highly effective chemical peptide ligation involving the ligation of peptides with C‐terminal salicylaldehyde esters to peptides with N‐terminal cysteine/penicillamine. The notable features of this method include its tolerance of steric hinderance from the side groups on either ligating terminus, thereby allowing flexible disconnection at sites that are otherwise difficult to functionalize. In addition, this method can be expanded to selective desulfurization and one‐pot ligation‐desulfurization reactions. The effectiveness of this method was demonstrated by the synthesis of VISTA (216‐311), PD‐1 (192‐288) and Eglin C.
Persistent Identifierhttp://hdl.handle.net/10722/284022
ISSN

 

DC FieldValueLanguage
dc.contributor.authorTan, Y-
dc.contributor.authorLI, J-
dc.contributor.authorJin, K-
dc.contributor.authorLIU, J-
dc.contributor.authorCHEN, Z-
dc.contributor.authorYang, J-
dc.contributor.authorLi, XC-
dc.date.accessioned2020-07-20T05:55:23Z-
dc.date.available2020-07-20T05:55:23Z-
dc.date.issued2020-
dc.identifier.citationAngewandte Chemie, 2020, v. 132 n. 31, p. 12841-12845-
dc.identifier.issn0044-8249-
dc.identifier.urihttp://hdl.handle.net/10722/284022-
dc.description.abstractThe chemical ligation of two unprotected peptides to generate a natural peptidic linkage specifically at the C‐ and N‐termini is a desirable goal in chemical protein synthesis but is challenging because it demands high reactivity and selectivity (chemo‐, regio‐, and stereoselectivity). We report an operationally simple and highly effective chemical peptide ligation involving the ligation of peptides with C‐terminal salicylaldehyde esters to peptides with N‐terminal cysteine/penicillamine. The notable features of this method include its tolerance of steric hinderance from the side groups on either ligating terminus, thereby allowing flexible disconnection at sites that are otherwise difficult to functionalize. In addition, this method can be expanded to selective desulfurization and one‐pot ligation‐desulfurization reactions. The effectiveness of this method was demonstrated by the synthesis of VISTA (216‐311), PD‐1 (192‐288) and Eglin C.-
dc.languageeng-
dc.publisherWiley - V C H Verlag GmbH & Co. KGaA. The Journal's web site is located at http://www.angewandte.de-
dc.relation.ispartofAngewandte Chemie-
dc.rightsThis is the peer reviewed version of the following article: [FULL CITE], which has been published in final form at [Link to final article using the DOI]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.-
dc.subjectchemical ligation-
dc.subjectchemical protein synthesis-
dc.subjectpeptide desulfurization-
dc.subjectpeptides-
dc.subjectproteins-
dc.titleCysteine/Penicillamine Ligation Independent of Terminal Steric Demands for Chemical Protein Synthesis-
dc.typeArticle-
dc.identifier.emailTan, Y: tanyi@hku.hk-
dc.identifier.emailYang, J: juny@hku.hk-
dc.identifier.emailLi, XC: xuechenl@hku.hk-
dc.identifier.authorityYang, J=rp02186-
dc.identifier.authorityLi, XC=rp00742-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/ange.202003652-
dc.identifier.scopuseid_2-s2.0-85088290888-
dc.identifier.hkuros311136-
dc.identifier.volume132-
dc.identifier.issue31-
dc.identifier.spage12841-
dc.identifier.epage12845-
dc.publisher.placeGermany-

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