Linked Life Data

1895300

Source:http://linkedlifedata.com/resource/pubmed/id/1895300

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1991-10-22
pubmed:abstractText
The C-terminal "address" sequences of prodynorphin-derived opioid peptides contain an unusually high proportion of basic residues, which are known to be crucial for conferring high activity and selectivity for kappa-opioid receptors. In an effort to investigate the possibility that the polycationic "tails" may be involved in a coulombic interaction with a complementary polyanionic receptor domain, we attached a series of achiral peptide-like cationic fragments to the C-terminus of the opioid peptide "message", Tyr-Gly-Gly-Phe. Binding of the various compounds to opioid receptor types in guinea pig brain membranes was weak, and the pharmacologic activities in the guinea pig ileum were marginal. These results indicate either that the chosen ligand design does not satisfy the structural requirements of the hypothesized coulombic interaction or that the latter is a minor criterion governing receptor recognition.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2816-21
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Modification of the enkephalin "message" with an artificial polycationic C-terminus.
pubmed:affiliation
Department of Chemistry, Case Western Reserve University, Cleveland, Ohio 44106-7078.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't