Protein β-interfaces as a generic source of native peptide tectons

Chem Commun (Camb). 2013 Apr 7;49(27):2825-7. doi: 10.1039/c3cc39052g.

Abstract

Motifs of 7-8 amino acids were designed from the β-continuous interfaces of non-related homo-oligomeric proteins. These peptides intrinsically self-assembled into nanoarchitectures in water, while retaining some properties of their parent interfaces, especially reversibility of assembly. These results reveal a novel source of native peptide tectons.

MeSH terms

  • Animals
  • Carboxy-Lyases / chemistry*
  • Carboxy-Lyases / metabolism
  • Cattle
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism
  • Lactoglobulins / chemistry*
  • Lactoglobulins / metabolism
  • Models, Molecular
  • Nanostructures / chemistry*
  • Peptide Fragments / chemistry*
  • Peroxiredoxin III / chemistry*
  • Peroxiredoxin III / metabolism
  • Protein Conformation
  • Protein Multimerization
  • Water / chemistry*

Substances

  • Escherichia coli Proteins
  • Lactoglobulins
  • Peptide Fragments
  • Water
  • Peroxiredoxin III
  • Carboxy-Lyases
  • LysA protein, E coli