The complete chirospectroscopic signature of the peptide 3(10)-helix in aqueous solution

Biopolymers. 2004 Sep;75(1):32-45. doi: 10.1002/bip.20109.

Abstract

We synthesized by solution methods a water-soluble, terminally blocked heptapeptide based on five markedly helicogenic, C(alpha)-tetrasubstituted alpha-amino acids C(alpha)-methyl-L-norvalines and two strongly hydrophilic 2-amino-3-[1-(1,4,7-triazacyclononane)]-L-propanoic acid residues at positions 2 and 5. A Fourier transform infrared absorption and NMR analysis in deuterated chloroform and aqueous solutions of the heptapeptide and two side-chain protected synthetic precursors confirmed our working hypothesis that all oligomers are folded in the 3(10)-helical conformation. Based on these findings, we exploited this heptapeptide as a chiral reference compound for detailed electronic CD, vibrational CD, and Raman optical activity characterizations of the 3(10)-helix in aqueous solution.

Publication types

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

MeSH terms

  • Circular Dichroism
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Oligopeptides / chemical synthesis
  • Oligopeptides / chemistry*
  • Protein Structure, Secondary
  • Stereoisomerism

Substances

  • Oligopeptides