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Extended Diethylglycine Homopeptides Formed by Desulfurization of Their Tetrahydrothiopyran Analogues

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)2209-2212
Number of pages4
JournalOrganic Letters
Volume21
Issue number7
Early online date12 Mar 2019
DOIs
DateAccepted/In press - 12 Mar 2019
DateE-pub ahead of print - 12 Mar 2019
DatePublished (current) - 5 Apr 2019

Abstract

Diethylglycine (Deg) homopeptides adopt the rare 2.0 5 -helical conformation, the longest three-dimensional structure that a peptide of a given sequence can adopt. Despite this unique conformational feature, Deg is rarely used in peptide design because of its poor reactivity. In this paper, we show that reductive desulfurization of oligomers formed from more reactive tetrahydrothiopyran-containing precursors provides a practical way to build the longest Deg homopeptides so far made, and we detail some conformational studies of the Deg oligomers and their heterocyclic precursors.

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    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via ACS at https://pubs.acs.org/doi/10.1021/acs.orglett.9b00501 . Please refer to any applicable terms of use of the publisher.

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