The twists and turns of beta-peptides

J Pept Res. 1999 Sep;54(3):206-17. doi: 10.1034/j.1399-3011.1999.00131.x.

Abstract

Recently, it has been discovered that peptides composed of beta-amino acids are capable of adopting novel secondary structures demonstrating that peptides composed of alpha-amino acids are not unique in their ability to fold into well-defined structures. Cyclic as well as acyclic peptides composed of beta-amino acid residues adopt turn, helical, and sheet-like conformations. Here, we discuss the synthesis and conformational preferences of individual, substituted beta-amino acids as well as the structures that peptides composed of these residues, beta-peptides, may adopt.

Publication types

  • Review

MeSH terms

  • Amino Acids / chemistry*
  • Circular Dichroism
  • Crystallography, X-Ray
  • Magnetic Resonance Spectroscopy
  • Models, Structural
  • Peptides / chemical synthesis
  • Peptides / chemistry*
  • Protein Conformation
  • Protein Engineering / methods
  • Protein Structure, Secondary

Substances

  • Amino Acids
  • Peptides