"Threading" of beta-sheet peptides via radical polymerization

Biomacromolecules. 2007 Feb;8(2):318-21. doi: 10.1021/bm060835n.

Abstract

A nonamer peptide containing a diene group in the center of the sequence was synthesized. When the peptide forms an antiparallel beta-sheet, the diene groups align ca. 5 A apart on the beta-sheet. The diene groups successfully photopolymerized without distorting the beta-sheet structure. The obtained beta-sheet showed high stability against acid denaturation and addition of 1,1,1,3,3,3-hexafluoroisopropanol.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkadienes
  • Peptides / chemistry*
  • Photochemistry
  • Propanols
  • Protein Denaturation
  • Protein Structure, Secondary

Substances

  • Alkadienes
  • Peptides
  • Propanols
  • hexafluoroisopropanol