Linked Life Data

21262295

Source:http://linkedlifedata.com/resource/pubmed/id/21262295

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2011-3-18
pubmed:abstractText
As part of ongoing work aimed at generating proteolytically stable, readily applicable, radiolabeled endomorphin-2 (EM-2) analogs for elucidation of the topological requirements of peptide binding to ?-opioid receptors, we report here on the synthesis, radiolabeling, binding kinetics and binding site distribution of an EM-2 analog in which Pro(2) is replaced by 2-aminocyclohexanecarboxylic acid, ACHC. [(3)H][(1S,2R)ACHC](2)EM-2 (specific activity 63.49Ci × mmol(-1)) bound specifically to its binding sites with high affinity (K(D) = 0.55 ± 0.06 nM) and saturably, yielding a receptor density, B(max) of 151 ± 4 fmol × mg protein(-1) in rat brain membranes. A similar affinity value was obtained in kinetic assays. Both Na(+) and Gpp(NH)p decreased the affinity, proving the agonist character of the radioligand. Specific ?-opioid ligands displaced the radioligand with much higher affinities than did ?- and ?-ligands. The autoradiographic distribution of the binding sites of [(3)H][(1S,2R)ACHC](2)EM-2 agreed well with the known locations of the ?-opioid receptors in the rat brain. In consequence of its high affinity, selectivity and enzymatic resistance [19], the new radioligand will be a good tool in studies of the topographical requirements of ?-opioid-specific peptide binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1873-5169
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
722-8
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Pharmacology of a new tritiated endomorphin-2 analog containing the proline mimetic cis-2-aminocyclohexanecarboxylic acid.
pubmed:affiliation
Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't