Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10836033 | Peptides | 2005 | 11 Pages |
Abstract
A novel hypothalamic neuropeptide of the RFamide family, comprising 26 amino acids residues and thus termed 26RFa, has been recently characterized in human, and was found to be the endogenous ligand for the orphan G protein-coupled receptor GPR103. Intracerebroventricular injection of 26RFa provokes a robust increase in food intake in rodents. In the present study, we have investigated the solution conformation of 26RFa by using two-dimensional NMR spectroscopy in different media. In water, 26RFa exhibits mainly a random coil conformation although the presence of a nascent helix was detected between residues 6 and 15. In methanol, 26RFa adopts a well-defined conformation consisting of an amphipathic α-helical structure (Pro4-Arg17), flanked by two N- and C-terminal disordered regions. The strong conservation, from amphibians to mammals, of the amino acid sequence corresponding to the amphipathic helix and to the C-terminal flexible octapeptide of 26RFa, suggests that these two domains are crucial for the interaction of the peptide with its receptor.
Keywords
SDSRMSDHMBCMALDI/TOF-MSHSQCFMOCTOCSYTPPINOESYNOERFamide-related peptide1H NMRNuclear Overhauser Effect SpectroscopYnuclear overhauser effecttime-proportional phase incrementationroot-mean-square deviationcircular dichroismSolution structuresodium dodecyl sulfateTotal correlation spectroscopycorrelated spectroscopyfluorenylmethoxycarbonylMolecular modelingNeuropeptideheteronuclear multiple-bond correlationCOSYheteronuclear single quantum coherence
Related Topics
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Biochemistry
Authors
Romain Thuau, Laure Guilhaudis, Isabelle Ségalas-Milazzo, Nicolas Chartrel, Hassan Oulyadi, Stéphane Boivin, Alain Fournier, Jérôme Leprince, Daniel Davoust, Hubert Vaudry,