Mimicry of a β-Hairpin Turn by a Nonpeptidic Laterally Flexible Foldamer

Joseph W. Meisel; Chunhua T. Hu; Andrew D. Hamilton

doi:10.1021/acs.orglett.8b01463

Mimicry of a β-Hairpin Turn by a Nonpeptidic Laterally Flexible Foldamer

Joseph W. Meisel, Chunhua T. Hu, Andrew D. Hamilton

Chemistry

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

Abstract

The design and characterization of a proteomimetic foldamer that displays lateral flexibility endowed by intramolecular bifurcated hydrogen bonds is reported. The MAMBA scaffold, derived from meta-aminomethylbenzoic acid, adopts a serpentine conformation that mimics the side chain projection of all four residues in a β-hairpin turn.

Original language	English (US)
Pages (from-to)	3879-3882
Number of pages	4
Journal	Organic Letters
Volume	20
Issue number	13
DOIs	https://doi.org/10.1021/acs.orglett.8b01463
State	Published - Jul 6 2018

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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10.1021/acs.orglett.8b01463

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title = "Mimicry of a β-Hairpin Turn by a Nonpeptidic Laterally Flexible Foldamer",

abstract = "The design and characterization of a proteomimetic foldamer that displays lateral flexibility endowed by intramolecular bifurcated hydrogen bonds is reported. The MAMBA scaffold, derived from meta-aminomethylbenzoic acid, adopts a serpentine conformation that mimics the side chain projection of all four residues in a β-hairpin turn.",

author = "Meisel, {Joseph W.} and Hu, {Chunhua T.} and Hamilton, {Andrew D.}",

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AB - The design and characterization of a proteomimetic foldamer that displays lateral flexibility endowed by intramolecular bifurcated hydrogen bonds is reported. The MAMBA scaffold, derived from meta-aminomethylbenzoic acid, adopts a serpentine conformation that mimics the side chain projection of all four residues in a β-hairpin turn.

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Mimicry of a β-Hairpin Turn by a Nonpeptidic Laterally Flexible Foldamer

Abstract

ASJC Scopus subject areas

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