Formation of an extremely stable polyalanine β-sheet macromolecule Article

Forood, B, Pérez-Payá, E, Houghten, RA et al. (1995). Formation of an extremely stable polyalanine β-sheet macromolecule . BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 211(1), 7-13. 10.1006/bbrc.1995.1770

cited authors

  • Forood, B; Pérez-Payá, E; Houghten, RA; Blondelle, SE

authors

abstract

  • We have designed a 16-mer peptide composed of a stretch of alanine residues (Ac-KA14K-NH2) which is an effective, simple model for the study of β-sheet formation in the hydrophobic cores of proteins. This peptide adopts an aqueous soluble 'bundling' macromolecular β-sheet structure, which is extremely stable to a wide range of pHs, temperatures and/or denaturants. Its unusual stability appears to be due to tight hydrophobic packing of the alanine residues in multilayer sheets or micellar forms with the multimeric lysine array being directed outward at the aqueous environment, allowing aqueous solubility. © 1995 Academic Press, Inc.

publication date

  • January 1, 1995

published in

Digital Object Identifier (DOI)

start page

  • 7

end page

  • 13

volume

  • 211

issue

  • 1