Further investigations on the optical activity of aromatic residues in Cyclolinopeptide a analogues

I. Z. Siemion, M. Cebrat, M. Lisowski

Research output: Contribution to journalArticlepeer-review

Abstract

CD spectra of a series of cyclolinopeptide A (CLA) analogues ([Ala1]CLA, [Ala7]CLA, [Ala1.7]CLA, [Ala8]CLA, [Ala9]CLA, [Ala8, Tyr9]CLA, [Ala9, Tyr8]CLA, and [Ala7, Phe(SO3Na)9]CLA) in methanol solution were analyzed. It was confirmed that the aromatic residue in position 9 contributes to a low extent only to the optical activity of the peptide. However, this phenomenon is not a result of the "edge-to-face" interaction of aromatic side chains but rather of the conformation of the aromatic side chain in position 9. This conclusion is confirmed by the fact that the decrease of the optical activity in that position was also observed in the spectra of analogues with only one aromatic residue. Analysis of the CD spectra reveals also that, contrary to Leu1, the Pro7 residue of the fragment -Pro-Phe-Phe-Leu-is a factor that determines the conformation of the peptide backbone and, in the consequence, the conformation of aromatic residues.

Original languageEnglish (US)
Pages (from-to)955-964
Number of pages10
JournalPolish Journal of Chemistry
Volume74
Issue number7
StatePublished - 2000
Externally publishedYes

Keywords

  • Circular dichroism
  • Conformation
  • Cyclic peptides
  • Cyclolinopeptide a
  • Edge-to-face interaction
  • Optical activity of aromatic amino acids

ASJC Scopus subject areas

  • Chemistry(all)

Fingerprint Dive into the research topics of 'Further investigations on the optical activity of aromatic residues in Cyclolinopeptide a analogues'. Together they form a unique fingerprint.

Cite this