Conformational study of three endothelin antagonists with 1H NMR at low temperature and molecular dynamics.
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.
Verheyden
P
P
Department of Organic Chemistry, Vrije Universiteit Brussel, Belgium.
Van Assche
I
I
Brichard
M H
MH
Demaude
T
T
Paye
I
I
Scarso
A
A
Van Binst
G
G
D000595:Amino Acid Sequence; D003080:Cold Temperature; D016232:Endothelins / Q000037:antagonists & inhibitors*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D010456:Peptides, Cyclic / Q000737:chemistry; D011487:Protein Conformation
D016232:Endothelins; D009842:Oligopeptides; D010456:Peptides, Cyclic; C087220:BQ 610; C072247:cyclo(Trp-Asp-Pro-Val-Leu)