Conformational study of three endothelin antagonists with 1H NMR at low temperature and molecular dynamics

P Verheyden; I Van Assche; M H Brichard; T Demaude; I Paye; A Scarso; G Van Binst

doi:10.1016/0014-5793(94)00352-1

Conformational study of three endothelin antagonists with 1H NMR at low temperature and molecular dynamics

FEBS Lett. 1994 May 9;344(1):55-60. doi: 10.1016/0014-5793(94)00352-1.

Authors

P Verheyden¹, I Van Assche, M H Brichard, T Demaude, I Paye, A Scarso, G Van Binst

Affiliation

¹ Department of Organic Chemistry, Vrije Universiteit Brussel, Belgium.

PMID: 8181565
DOI: 10.1016/0014-5793(94)00352-1

Abstract

The conformations of three endothelin antagonists, a cyclic pentapeptide, a linear tripeptide and a linear hexapeptide, are compared by 1H NMR and molecular dynamics. The three analogues have a Leu and a DTrp side chain which are oriented parallel, and an acidic group next to the DTrp residue.

MeSH terms

Amino Acid Sequence
Cold Temperature*
Endothelins / antagonists & inhibitors*
Magnetic Resonance Spectroscopy*
Molecular Sequence Data
Oligopeptides / chemistry
Peptides, Cyclic / chemistry
Protein Conformation

Substances

Endothelins
Oligopeptides
Peptides, Cyclic
BQ 610
cyclo(Trp-Asp-Pro-Val-Leu)