title: Conformational study of three endothelin antagonists with 1H NMR at low temperature and molecular dynamics.
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.
authors.affiliation: Department of Organic Chemistry, Vrije Universiteit Brussel, Belgium.
authors.forename: P
authors.initials: P
authors.lastname: Verheyden
authors.forename: I
authors.initials: I
authors.lastname: Van Assche
authors.forename: M H
authors.initials: MH
authors.lastname: Brichard
authors.forename: T
authors.initials: T
authors.lastname: Demaude
authors.forename: I
authors.initials: I
authors.lastname: Paye
authors.forename: A
authors.initials: A
authors.lastname: Scarso
authors.forename: G
authors.initials: G
authors.lastname: Van Binst
mesh_terms: 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
chemical_list: D016232:Endothelins; D009842:Oligopeptides; D010456:Peptides, Cyclic; C087220:BQ 610; C072247:cyclo(Trp-Asp-Pro-Val-Leu)