Linked Life Data

8060305

Source:http://linkedlifedata.com/resource/pubmed/id/8060305

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-9-12
pubmed:abstractText
Opioid receptor antagonist properties of the mu opioid receptor selective peptide, BOC-Tyr-Lys-Lys-Trp-Trp-NH2 and its systematically modified analogues were determined in guinea pig ileum, mouse vas deferens and rabbit vas deferens bioassays to locate the necessary structural features to develop kappa receptor selective antagonist(s) of substantial affinity. Replacing the tyrosine residue by phenylalanine as well as increasing the lipophilicity of the C-terminal by isoamylamide substitution yielded enhanced kappa receptor affinity. The presence of the C-terminal lipophilic Trp-Trp-NH2 region is necessary as revealed from the equilibrium dissociation constant values. Recognizing that only one lysine residue is required for the antagonist activity led to the synthesis of the tetrapeptide BOC-Tyr-Lys-Trp-Trp-NH2 having a kappa/mu selectivity of 22 and a Ke of 5.4 microM.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
202
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1285-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
N-terminally protected penta- and tetrapeptide opioid antagonists based on a pentapeptide sequence found in the venom of Philippine cobra.
pubmed:affiliation
Research Group of Peptide Chemistry, Hungarian Academy of Sciences, Budapest.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't