Source:http://linkedlifedata.com/resource/pubmed/id/20936621
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2010-10-28
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pubmed:abstractText |
Herein we describe the synthesis and HIV-1 protease (PR) inhibitory activity of 16 new peptidomimetic molecular tongs with a naphthalene scaffold. Their peptidic character was progressively decreased. Two of these molecules exhibited the best dimerization inhibition activity toward HIV-1 wild-type and multimutated ANAM-11 proteases obtained to date for this class of molecules (?40?nM for wild-type PR and 100?nM for ANAM-11 PR). Although the peptidic character of one molecular tong was completely suppressed, the mechanism of inhibition and inhibitory potency toward both proteases were maintained.
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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 |
Nov
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pubmed:issn |
1860-7187
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
8
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1899-906
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pubmed:meshHeading |
pubmed-meshheading:20936621-HIV Infections,
pubmed-meshheading:20936621-HIV Protease,
pubmed-meshheading:20936621-HIV Protease Inhibitors,
pubmed-meshheading:20936621-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:20936621-Inhibitory Concentration 50,
pubmed-meshheading:20936621-Molecular Mimicry,
pubmed-meshheading:20936621-Mutation,
pubmed-meshheading:20936621-Naphthalenes,
pubmed-meshheading:20936621-Protein Binding,
pubmed-meshheading:20936621-Protein Multimerization
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pubmed:year |
2010
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pubmed:articleTitle |
Toward the first nonpeptidic molecular tong inhibitor of wild-type and mutated HIV-1 protease dimerization.
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pubmed:affiliation |
Molécules Fluorées et Chimie Médicinale, BioCIS UMR-CNRS 8076, IPSIT, Université Paris-Sud 11, Faculté de Pharmacie, 5 rue Jean-Baptiste Clément, 92296, Châtenay-Malabry Cedex, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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