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Extended Diethylglycine Homopeptides Formed by Desulfurization of Their Tetrahydrothiopyran Analogues

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Extended Diethylglycine Homopeptides Formed by Desulfurization of Their Tetrahydrothiopyran Analogues. / De Zotti, Marta; Clayden, Jonathan.

In: Organic Letters, Vol. 21, No. 7, 05.04.2019, p. 2209-2212.

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@article{01d337be8f114323a5bf3c367e33d815,
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.",
author = "{De Zotti}, Marta and Jonathan Clayden",
year = "2019",
month = "4",
day = "5",
doi = "10.1021/acs.orglett.9b00501",
language = "English",
volume = "21",
pages = "2209--2212",
journal = "Organic Letters",
issn = "1523-7060",
publisher = "American Chemical Society",
number = "7",

}

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TY - JOUR

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.

UR - http://www.scopus.com/inward/record.url?scp=85063932848&partnerID=8YFLogxK

U2 - 10.1021/acs.orglett.9b00501

DO - 10.1021/acs.orglett.9b00501

M3 - Article

VL - 21

SP - 2209

EP - 2212

JO - Organic Letters

JF - Organic Letters

SN - 1523-7060

IS - 7

ER -