Design, synthesis and protein-targeting properties of thioether-linked hydrogen bond surrogate helices

Andrew B. Mahon; Paramjit S. Arora

doi:10.1039/c1cc14730g

Design, synthesis and protein-targeting properties of thioether-linked hydrogen bond surrogate helices

Andrew B. Mahon
, Paramjit S. Arora

Research output: Contribution to journal › Article › peer-review

44 Scopus citations

Abstract

Appropriately-placed hydrogen bond surrogates have been demonstrated to efficiently nucleate helical conformations. Herein we describe an efficient method for the synthesis of thioether-based hydrogen bond surrogate (teHBS) helices. A teHBS helix is shown to adopt a stable conformation and target its cognate protein receptor with high affinity.

Original language	English
Pages (from-to)	1416-1418
Number of pages	3
Journal	Chemical Communications
Volume	48
Issue number	10
DOIs	https://doi.org/10.1039/c1cc14730g
State	Published - 11 Jan 2012
Externally published	Yes

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title = "Design, synthesis and protein-targeting properties of thioether-linked hydrogen bond surrogate helices",

abstract = "Appropriately-placed hydrogen bond surrogates have been demonstrated to efficiently nucleate helical conformations. Herein we describe an efficient method for the synthesis of thioether-based hydrogen bond surrogate (teHBS) helices. A teHBS helix is shown to adopt a stable conformation and target its cognate protein receptor with high affinity.",

author = "Mahon, \{Andrew B.\} and Arora, \{Paramjit S.\}",

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T1 - Design, synthesis and protein-targeting properties of thioether-linked hydrogen bond surrogate helices

AU - Mahon, Andrew B.

AU - Arora, Paramjit S.

PY - 2012/1/11

Y1 - 2012/1/11

N2 - Appropriately-placed hydrogen bond surrogates have been demonstrated to efficiently nucleate helical conformations. Herein we describe an efficient method for the synthesis of thioether-based hydrogen bond surrogate (teHBS) helices. A teHBS helix is shown to adopt a stable conformation and target its cognate protein receptor with high affinity.

AB - Appropriately-placed hydrogen bond surrogates have been demonstrated to efficiently nucleate helical conformations. Herein we describe an efficient method for the synthesis of thioether-based hydrogen bond surrogate (teHBS) helices. A teHBS helix is shown to adopt a stable conformation and target its cognate protein receptor with high affinity.

UR - https://www.scopus.com/pages/publications/84855647628

U2 - 10.1039/c1cc14730g

DO - 10.1039/c1cc14730g

M3 - Article

C2 - 21952530

AN - SCOPUS:84855647628

SN - 1359-7345

VL - 48

SP - 1416

EP - 1418

JO - Chemical Communications

JF - Chemical Communications

IS - 10

ER -

Design, synthesis and protein-targeting properties of thioether-linked hydrogen bond surrogate helices

Abstract

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