Source:http://linkedlifedata.com/resource/pubmed/id/18062664
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2008-1-3
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| pubmed:abstractText |
The constitutional similarity with different secondary structure preference between the Aba-Gly and the spiro-Aba-Gly scaffolds were exploited to design the novel endomorphin-2 analogs Tyr-spiro-( R/ S)-Aba-Gly-Phe-NH(2) ( 1 and 2) and Tyr-( R/ S)-Aba-Gly-Phe-NH(2) ( 3 and 4). The ( R)-spiro analog 1 was found to be a potent and selective micro-opioid agonist/partial agonist ( K (imicro) = 29.3 nM, IC(50) = 50 nM, K(e) = 0.57). NMR experiments and molecular modeling indicated that its backbone adopts mainly a beta-turn in aqueous solution.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
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| pubmed:issn |
0022-2623
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| pubmed:author |
pubmed-author:Al-KhrasaniMahmoudM,
pubmed-author:BalletStevenS,
pubmed-author:BenyheSándorS,
pubmed-author:BoricsAttilaA,
pubmed-author:FürstZsuzsannaZ,
pubmed-author:FeytensDebbyD,
pubmed-author:KövérKatalin EKE,
pubmed-author:LovasSándorS,
pubmed-author:TóthGézaG,
pubmed-author:TömbölyCsabaC,
pubmed-author:TourwéDirkD
|
| pubmed:issnType |
Print
|
| pubmed:day |
10
|
| pubmed:volume |
51
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
173-7
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| pubmed:meshHeading |
pubmed-meshheading:18062664-Magnetic Resonance Spectroscopy,
pubmed-meshheading:18062664-Models, Molecular,
pubmed-meshheading:18062664-Oligopeptides,
pubmed-meshheading:18062664-Protein Structure, Secondary,
pubmed-meshheading:18062664-Receptors, Opioid, mu,
pubmed-meshheading:18062664-Solutions,
pubmed-meshheading:18062664-Stereoisomerism,
pubmed-meshheading:18062664-Structure-Activity Relationship
|
| pubmed:year |
2008
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| pubmed:articleTitle |
Endomorphin-2 with a beta-turn backbone constraint retains the potent micro-opioid receptor agonist properties.
|
| pubmed:affiliation |
Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, Temesvári krt. 62., H-6726 Szeged, Hungary. tomboly@brc.hu
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|