Extended Diethylglycine Homopeptides Formed by Desulfurization of Their Tetrahydrothiopyran Analogues

Marta De Zotti*, Jonathan Clayden

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)

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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.

Original languageEnglish
Pages (from-to)2209-2212
Number of pages4
JournalOrganic Letters
Volume21
Issue number7
Early online date12 Mar 2019
DOIs
Publication statusPublished - 5 Apr 2019

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