Extended Diethylglycine Homopeptides Formed by Desulfurization of Their Tetrahydrothiopyran Analogues

Marta De Zotti; Jonathan Clayden

doi:10.1021/acs.orglett.9b00501

Extended Diethylglycine Homopeptides Formed by Desulfurization of Their Tetrahydrothiopyran Analogues

Marta De Zotti^*, Jonathan Clayden

^*Corresponding author for this work

School of Chemistry

Research output: Contribution to journal › Article (Academic Journal) › peer-review

2 Citations (Scopus)

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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 language	English
Pages (from-to)	2209-2212
Number of pages	4
Journal	Organic Letters
Volume	21
Issue number	7
Early online date	12 Mar 2019
DOIs	https://doi.org/10.1021/acs.orglett.9b00501
Publication status	Published - 5 Apr 2019

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title = "Extended Diethylglycine Homopeptides Formed by Desulfurization of Their Tetrahydrothiopyran Analogues",

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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doi = "10.1021/acs.orglett.9b00501",

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T1 - Extended Diethylglycine Homopeptides Formed by Desulfurization of Their Tetrahydrothiopyran Analogues

AU - De Zotti, Marta

AU - Clayden, Jonathan

PY - 2019/4/5

Y1 - 2019/4/5

N2 - 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.

AB - 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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U2 - 10.1021/acs.orglett.9b00501

DO - 10.1021/acs.orglett.9b00501

M3 - Article (Academic Journal)

C2 - 30859838

AN - SCOPUS:85063932848

VL - 21

SP - 2209

EP - 2212

JO - Organic Letters

JF - Organic Letters

SN - 1523-7060

IS - 7

ER -

Extended Diethylglycine Homopeptides Formed by Desulfurization of Their Tetrahydrothiopyran Analogues

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