title: Cyclic cholecystokinin-analog pentapeptide cyclo (Asp-Trp-Met-Asp-Phe): an unexpected solution conformation.
abstract: The conformational analysis of the CCK-B binding peptide cyclo (Asp-Trp-Met-Asp-Phe) has been carried out in DMSO-d6 and in a mixture of H2O/DMSO-d6 by NMR spectroscopy and by restrained molecular dynamics methods. In the NMR spectra, only one set of resonance signals was found. The NOE analyses proved the existence of an all-trans conformation for this peptide. Distance constraints of 1H pairs derived from NOE data were used for restrained molecular dynamics simulations, resulting in one conformational family with a very regular orientation of the amino acids and similar dihedral angles for each residue. The dihedrals and the absence of an intramolecular hydrogen bond indicate that there is no common turn formation in the peptide backbone. A submicromolar binding constant for CCK-B receptors point to a similarity with the bioactive conformation.
authors.affiliation: Humboldt Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, Institut für Chemie, Germany.
authors.forename: H
authors.initials: H
authors.lastname: Weisshoff
authors.forename: T
authors.initials: T
authors.lastname: Wieprecht
authors.forename: P
authors.initials: P
authors.lastname: Henklein
authors.forename: C
authors.initials: C
authors.lastname: Antz
authors.forename: C
authors.initials: C
authors.lastname: Mügge
mesh_terms: D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002766:Cholecystokinin / Q000031:analogs & derivatives*; D004121:Dimethyl Sulfoxide; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000737:chemistry*; D011487:Protein Conformation; D011522:Protons; D012996:Solutions
chemical_list: D010456:Peptides, Cyclic; D011522:Protons; D012996:Solutions; C095193:cyclo(aspartyl-tryptophyl-methionyl-aspartyl-phenylalanyl); D002766:Cholecystokinin; D004121:Dimethyl Sulfoxide