Linked Life Data

21548099

Source:http://linkedlifedata.com/resource/pubmed/id/21548099

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2011-5-27
pubmed:abstractText
Selectivity is a major issue in closely related multiligand/multireceptor systems. In this study we investigated the RFamide systems of hNPFF?R and hNPFF?R that bind the endogenous peptide hormones NPFF, NPAF, NPVF, and NPSF. By use of a systematic approach, we characterized the role of the C-terminal dipeptide with respect to agonistic properties using synthesized [Xaa?7]NPFF and [Xaa?8]NPFF analogues. We were able to identify only slight differences in potency upon changing the position of Arg?7, as all modifications resulted in identical behavior at the NPFF?R and NPFF?R. However, the C-terminal Phe?8 was able to be replaced by Trp or His with only a minor loss in potency at the NPFF?R relative to the NPFF?R. Analogues with shorter side chains, such as ?-amino-4-guanidino butyric acid ([Agb?7]NPFF) or phenylglycine ([Phg?8]NPFF), decreased efficacy for the NPFF? R to 25-31?% of the maximal response, suggesting that these agonist-receptor complexes are more susceptible to structural modifications. In contrast, mutations to the conserved Asp?6.59 residue in the third extracellular loop of both receptors revealed a higher sensitivity toward the hNPFF?R receptor than toward hNPFF?R. These data provide new insight into the subtype-specific agonistic activation of the NPFF? and NPFF(2) receptors that are necessary for the development of selective agonists.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1860-7187
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
pubmed:issnType
Electronic
pubmed:day
6
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1081-93
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Structure-activity studies of RFamide peptides reveal subtype-selective activation of neuropeptide FF1 and FF2 receptors.
pubmed:affiliation
Institute of Biochemistry, Faculty of Biosciences, Pharmacy and Psychology, Leipzig University, Brüderstraße 34, 04103 Leipzig, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't