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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
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Artificial β-Double Helices from Achiral γ-Peptides.

Rajkumar Misra1, Sanjit Dey1, Rahi M Reja1

  • 1Department of Chemistry, Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pune-, 411 008, India.

Angewandte Chemie (International Ed. in English)
|December 2, 2017
PubMed
Summary

Achiral gamma-peptides spontaneously form stable beta-double-helical structures, stabilized by backbone amide hydrogen bonds. These findings expand our understanding of peptide foldamers and their potential applications.

Keywords:
achiralityamino acidsfoldamerspeptidesβ-double helix

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Polymer Chemistry

Background:

  • Double helices are rare in natural polypeptides and proteins, with notable exceptions like gramicidin A.
  • Peptide foldamers offer diverse structural possibilities beyond natural amino acid polymers.

Purpose of the Study:

  • To investigate the spontaneous formation of double-helical structures in achiral gamma-peptides.
  • To characterize the structural stability and solution behavior of these novel peptide architectures.

Main Methods:

  • X-ray crystallography to determine solid-state structures.
  • Nuclear Magnetic Resonance (NMR) spectroscopy to analyze conformations in solution.
  • Fluorescence spectroscopy to study structural dynamics and stability.

Main Results:

  • Achiral gamma-peptides self-assemble into parallel beta-double helical structures.
  • Interstrand backbone amide hydrogen bonds are key stabilizing forces for these helices.
  • Solution studies confirm the existence and stability of double-helical conformations.

Conclusions:

  • Achiral gamma-peptides can spontaneously form beta-double helices, a previously unreported phenomenon.
  • This discovery expands the known repertoire of folded architectures in peptide foldamers.
  • The findings have implications for the design of novel peptide-based materials and therapeutics.