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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2008-5-12
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pubmed:abstractText |
A series of N-terminus benzamides of glycine-based symmetric peptides, linked to m-xylylenediamine and 3,4'-oxydianiline spacers, were prepared and tested as inhibitors of beta-amyloid peptide Abeta(1-40) aggregation in vitro. Compounds with good anti-aggregating activity were detected. Polyphenolic amides showed the highest anti-aggregating activity, with IC(50) values in the micromolar range. Structure-activity relationships suggested that pi-pi stacking and hydrogen-bonding interactions play a key role in the inhibition of Abeta(1-40) self-assembly leading to amyloid fibrils.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1,3-xylenediamine,
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Aniline Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Benzamides,
http://linkedlifedata.com/resource/pubmed/chemical/Caffeic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phenyl Ethers,
http://linkedlifedata.com/resource/pubmed/chemical/Xylenes,
http://linkedlifedata.com/resource/pubmed/chemical/amyloid beta-protein (1-40),
http://linkedlifedata.com/resource/pubmed/chemical/phenylethyl 3-methylcaffeate
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1464-3391
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4810-22
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:18406152-Amyloid beta-Peptides,
pubmed-meshheading:18406152-Aniline Compounds,
pubmed-meshheading:18406152-Benzamides,
pubmed-meshheading:18406152-Caffeic Acids,
pubmed-meshheading:18406152-Drug Design,
pubmed-meshheading:18406152-Glycine,
pubmed-meshheading:18406152-Molecular Structure,
pubmed-meshheading:18406152-Peptide Fragments,
pubmed-meshheading:18406152-Peptides,
pubmed-meshheading:18406152-Phenyl Ethers,
pubmed-meshheading:18406152-Stereoisomerism,
pubmed-meshheading:18406152-Structure-Activity Relationship,
pubmed-meshheading:18406152-Time Factors,
pubmed-meshheading:18406152-Xylenes
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pubmed:year |
2008
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pubmed:articleTitle |
Design, synthesis, and biological evaluation of glycine-based molecular tongs as inhibitors of Abeta1-40 aggregation in vitro.
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pubmed:affiliation |
Dipartimento Farmaco-chimico, Università degli Studi di Bari, Via Orabona 4, 70125 Bari, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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