rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2006-3-10
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pubmed:abstractText |
A designed library of tripeptidomimics of Ornithyl-Proline (Orn-Pro) and Lysyl-Proline (Lys-Pro) conjugated with various unnatural amino acids and carboxylic acid derived heterocyclics was synthesized and screened for possible inhibitors of angiotensin-converting enzyme (ACE). Among the tripeptidomimics 10[MTP-Orn-Pro], 11[HTP-Orn-Pro], 14[TA-Orn-Pro] and 20[BPA-Orn-Pro] showed prominent inhibition with IC50 values in micromolar concentrations. Structure-activity relationship study indicated that C3 side chain of Orn as compared to C4 side chain of Lys at P1' position was better suited to inhibit ACE, with propionic acid (C3) derived heterocyclics and unnatural amino acids.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Apr
|
pubmed:issn |
0960-894X
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
15
|
pubmed:volume |
16
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
2117-21
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pubmed:dateRevised |
2006-7-10
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pubmed:meshHeading |
pubmed-meshheading:16464585-Angiotensin-Converting Enzyme Inhibitors,
pubmed-meshheading:16464585-Animals,
pubmed-meshheading:16464585-Binding Sites,
pubmed-meshheading:16464585-Cattle,
pubmed-meshheading:16464585-Kidney,
pubmed-meshheading:16464585-Lysine,
pubmed-meshheading:16464585-Molecular Mimicry,
pubmed-meshheading:16464585-Oligopeptides,
pubmed-meshheading:16464585-Ornithine,
pubmed-meshheading:16464585-Proline,
pubmed-meshheading:16464585-Structure-Activity Relationship
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pubmed:year |
2006
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pubmed:articleTitle |
Structure-activity relationship study between Ornithyl-Proline and Lysyl-Proline based tripeptidomimics as angiotensin-converting enzyme inhibitors.
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pubmed:affiliation |
Peptide Synthesis Lab, Institute of Genomics and Integrative Biology, Mall Road, Delhi 110007, India.
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pubmed:publicationType |
Journal Article
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