Toward beta-amino acid proteins: design, synthesis, and characterization of a fifteen kilodalton beta-peptide tetramer

J Am Chem Soc. 2008 Jan 23;130(3):821-3. doi: 10.1021/ja077245x. Epub 2008 Jan 1.

Abstract

A 28 residue "retro" beta-peptide has been designed to self-assemble as a tetramer, successfully recapitulating the octameric beta-peptide bundle complex Zwit-1F. Z28, the largest beta-peptide synthesized to date, was achieved in a linear, microwave-assisted synthesis in 19% isolated yield and high purity. Z28 forms the expected tetrameric complex and is more stable and cooperative in its folding than Zwit-1F. The successful design and synthesis of Z28 is an important step toward true beta-amino acid proteins.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / chemistry*
  • Molecular Sequence Data
  • Molecular Weight
  • Peptides / chemistry*
  • Protein Conformation
  • Protein Structure, Secondary
  • Proteins / chemistry*

Substances

  • Amino Acids
  • Peptides
  • Proteins
  • Z28 peptide