Studies related to the relative thermodynamic stability of C-terminal peptidyl esters of O-hydroxy thiophenol: Emergence of a doable strategy for non-cysteine ligation applicable to the chemical synthesis of glycopeptides Journal Article

  

Authors:	Chen, G.; David Warren, J.; Chen, J.; Wu, B.; Wan, Q.; Danishefsky, S. J.
Article Title:	Studies related to the relative thermodynamic stability of C-terminal peptidyl esters of O-hydroxy thiophenol: Emergence of a doable strategy for non-cysteine ligation applicable to the chemical synthesis of glycopeptides
Abstract:	A pathway has been devised, wherein a phenolic ester of a C-terminal peptide is ligated with an N-terminal peptide through two consecutive acyl migrations. In the first transacylation, the C-terminus is transferred from a phenol to a newly liberated ortho-thiol function. Subsequently, the acyl group is transported to a proximal benzylamine through a six-membered transition state. Copyright © 2006 American Chemical Society.
Keywords:	carboxy terminal sequence; magnetic resonance spectroscopy; thermodynamics; phenols; reaction analysis; models, chemical; glycopeptide; glycopeptides; cysteine; peptide synthesis; stereoisomerism; esters; carbon nuclear magnetic resonance; thiophenol derivative; ester derivative; molecular stability; sulfhydryl compounds
Journal Title:	Journal of the American Chemical Society
Volume:	128
Issue:	23
ISSN:	0002-7863
Publisher:	American Chemical Society
Date Published:	2006-06-14
Start Page:	7460
End Page:	7462
Language:	English
DOI:	10.1021/ja061588y
PUBMED:	16756298
PROVIDER:	scopus
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-33745046822&partnerID=40&md5=b4eb70907cbb7f938be6d7d735dff937
Notes:	--- - "Cited By (since 1996): 34" - "Export Date: 4 June 2012" - "CODEN: JACSA" - "Source: Scopus"

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