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Structure-Property Relationship Study of N-(Hydroxy)Peptides for the Design of Self-Assembled Parallel β-Sheets.

preprint
submitted on 15.06.2020, 22:38 and posted on 17.06.2020, 09:50 by Alexis Richaud, Stephane Roche
The design of novel and functional biomimetic foldamers remains a major challenge in creating mimics of native protein structures. Herein, we report the stabilization of a short b-sheet by incorporating N-(hydroxy)glycine (Hyg) residues into the backbone of peptides. These short peptide−peptoid hybrids form unique parallel b-sheet structures by self-assembly. Spectroscopic and crystallographic data collected suggest that the local conformational perturbations induced by N-(hydroxy)amides are outweighed by a network of strong interstrand hydrogen-bonds.

Funding

Flexible Rigidity in Peptide Drug Design for Protein-Protein Interaction Inhibitors

National Institute of General Medical Sciences

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History

Email Address of Submitting Author

sroche2@fau.edu

Institution

Florida Atlantic University

Country

United States

ORCID For Submitting Author

0000-0002-3019-2168

Declaration of Conflict of Interest

No conflict of interest

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