Linked Life Data

11745115

Source:http://linkedlifedata.com/resource/pubmed/id/11745115

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2001-12-17
pubmed:abstractText
Human ghrelin, the first recognized natural ligand of growth hormone secretagogue growth hormone secretagogue receptors (GHS-Rs) (M. Kojima, H. Hosada, Y. Date, M. Nakazato, H. Matsuo, and K. Kangawa, Nature, 1999, Vol. 402, pp. 656-660), consists of 28 amino acids of which Ser3 is modified by n-octanoylation. This new peptide hormone has been implicated not only in regulation of the GH secretion but also in regulation of food intake. The discovery of ghrelin opens up more opportunities to study the relationship of ghrelin with metabolic diseases. Until now, only mass spectometry analysis has been reported on the structure of ghrelin. NMR analysis is a suitable way to study if any tertiary structure of unbound ghrelin is present in solution. NMR studies were carried out on human ghrelin and its five truncated analogs. The full-length ghrelin and its fragments exhibited random coil behavior in aqueous solution. Additional studies were carried out on the shortest active segment of human ghrelin, which consists of the first five amino acids of the ghrelin sequence (M. A. Bednarek, S. D. Feighner, S.-S. Pong, K. K. McKee, D. L. Hreniuk, M. V. Silva, V. A. Warrem, A. D. Howard, L. H. Y. Van der Ploeg, and J. V. Heck, Journal of Medical Chemistry, 2000, Vol. 43, pp. 4370-4376), to compare the spectral features with their counterparts in the full-length ghrelin. The NMR data showed behavior similar to ghrelin except for two additional nuclear Overhauser effects (NOEs) between the Phe4 NH and the protons of the beta-methylene of Ser3. CD on human ghrelin and its short active analog in water were indicative of random coil peptides. Molecular modeling based on NMR data was carried out to probe which structural features were similar to growth hormone-releasing peptide-6 (GHRP-6), a hexapeptide that binds to GHS-R releasing GH and stimulating food intake. Modeling suggested some similarities, but they were not of a nature to account for binding properties of these compounds.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3525
pubmed:author
pubmed:copyrightInfo
Copyright 2001 John Wiley & Sons, Inc. Biopolymers 59: 489-501, 2001
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
489-501
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:11745115-Amino Acid Sequence, pubmed-meshheading:11745115-Circular Dichroism, pubmed-meshheading:11745115-Ghrelin, pubmed-meshheading:11745115-Growth Hormone, pubmed-meshheading:11745115-Hormones, pubmed-meshheading:11745115-Hot Temperature, pubmed-meshheading:11745115-Humans, pubmed-meshheading:11745115-Hydrogen-Ion Concentration, pubmed-meshheading:11745115-Ligands, pubmed-meshheading:11745115-Magnetic Resonance Spectroscopy, pubmed-meshheading:11745115-Models, Molecular, pubmed-meshheading:11745115-Molecular Sequence Data, pubmed-meshheading:11745115-Oligopeptides, pubmed-meshheading:11745115-Peptide Hormones, pubmed-meshheading:11745115-Peptides, pubmed-meshheading:11745115-Protein Folding, pubmed-meshheading:11745115-Protein Structure, Tertiary, pubmed-meshheading:11745115-Protons, pubmed-meshheading:11745115-Serine, pubmed-meshheading:11745115-Water
pubmed:year
2001
pubmed:articleTitle
1H NMR structural analysis of human ghrelin and its six truncated analogs.
pubmed:affiliation
Department of Drug Metabolism, Merck Research Laboratories, Rahway, NJ, USA. maria_silva1@merck.com
pubmed:publicationType
Journal Article, Comparative Study