Linked Life Data

3032674

Source:http://linkedlifedata.com/resource/pubmed/id/3032674

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-6-17
pubmed:abstractText
The opioid activity pattern of 8 dermorphin tetrapeptides, W-Tyr-D-MetO-Phe-Xaa-Y (W = H, H2N-C = (NH); Xaa = Gly, 2-aminoethanol, sarcosine; Y = NH2, NH-alkyl), was determined in guinea-pig ileum (GPI) preparations and in brain binding assays and compared with their antinociceptive potency in mice. Almost all modifications increased potency on the GPI test as well as the antinociceptive action of the parent H-Tyr-D-Ala-Phe-Gly-NH2. Dermorphin, H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2, and related tetrapeptide analogues show negligible K-binding activity and, like morphine, possess a higher affinity to mu- than delta-receptors. Nevertheless the correlation of analgesia with the effects on GPI and binding data separate the peptides from morphine. For example, in comparison with the opiate alkaloid H-Tyr-D-MetO-Phe-Gly-ol and H-Tyr-D-MetO-Phe-Gly-NH2 displayed a lower affinity for mu sites, a moderately higher potency on GPI but an exceptionally stronger analgesia, being respectively 350 and 1500 times as potent an analgesic as morphine. This may involve different subpopulations of opioid mu-receptors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0430-0920
pubmed:author
pubmed:issnType
Print
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
125-31
pubmed:dateRevised
2009-6-5
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Opioid peptides. Biological study of [D-MetO2] dermorphin analogues in relation to the plurality of opioid receptors. XI.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't