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

Chemistry

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

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 (US)
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 - Jan 11 2012

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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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.",

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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.

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

Abstract

ASJC Scopus subject areas

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