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

Org Lett. 2018 Jul 6;20(13):3879-3882. doi: 10.1021/acs.orglett.8b01463. Epub 2018 Jun 13.

Authors

Joseph W Meisel¹, Chunhua T Hu¹, Andrew D Hamilton¹

Affiliation

¹ Department of Chemistry , New York University , New York , New York 10003 , United States.

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.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Biomimetics
Hydrogen Bonding
Models, Molecular*
Molecular Conformation
Peptides

Substances

Peptides

Grants and funding

F32 GM126851/GM/NIGMS NIH HHS/United States