Comparison of the conformations of cyclolinopeptide A in the solid state and in solution

Biopolymers. 1989 Jan;28(1):513-23. doi: 10.1002/bip.360280145.

Abstract

Cyclolinopeptide A, a cyclic nonapeptide isolated from linseed, has lately attracted large interest for its cytoprotective activity. The recent elucidation of its solid state structure has prompted us to undertake a detailed conformational analysis in solution. Room-temperature 1H-nmr spectra in several solvents (DMSO-d6, DMSO-d6/D2O/H2O, CD3OH, (CD3)2CDOH, CDCl3) all show very broad lines, indicating the presence of chemical exchange among several conformers. It proved possible to freeze a single conformational state in CDCl3 at 214 K. Unusual chemical shifts and nuclear Overhauser enhancements are consistent with the main features of the solid state structure.

Publication types

  • Comparative Study

MeSH terms

  • Peptides, Cyclic* / chemical synthesis
  • Protein Conformation
  • Solutions

Substances

  • Peptides, Cyclic
  • Solutions
  • cyclolinopeptide A