Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane

Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3334-8. doi: 10.1073/pnas.90.8.3334.

Abstract

A 16-residue peptide [(Ala-Glu-Ala-Glu-Ala-Lys-Ala-Lys)2] has a characteristic beta-sheet circular dichroism spectrum in water. Upon the addition of salt, the peptide spontaneously assembles to form a macroscopic membrane. The membrane does not dissolve in heat or in acidic or alkaline solutions, nor does it dissolve upon addition of guanidine hydrochloride, SDS/urea, or a variety of proteolytic enzymes. Scanning EM reveals a network of interwoven filaments approximately 10-20 nm in diameter. An important component of the stability is probably due to formation of complementary ionic bonds between glutamic and lysine side chains. This phenomenon may be a model for studying the insoluble peptides found in certain neurological disorders. It may also have implications for biomaterials and origin-of-life research.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amyloid / chemistry
  • Circular Dichroism
  • Membranes, Artificial*
  • Molecular Sequence Data
  • Oligopeptides / chemical synthesis
  • Oligopeptides / chemistry*
  • Peptide Fragments / chemistry
  • Peptides / chemical synthesis
  • Peptides / chemistry*
  • Protein Conformation*
  • Structure-Activity Relationship
  • Substance P / analogs & derivatives
  • Substance P / chemistry

Substances

  • Amyloid
  • Membranes, Artificial
  • Oligopeptides
  • Peptide Fragments
  • Peptides
  • Substance P
  • spantide