Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amyloid beta-Peptides / antagonists & inhibitors*
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Amyloid beta-Peptides / chemistry*
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Aniline Compounds / chemistry
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Benzamides / chemical synthesis
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Benzamides / chemistry
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Benzamides / pharmacology*
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Caffeic Acids
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Drug Design
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Glycine / chemistry*
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Molecular Structure
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Peptide Fragments / antagonists & inhibitors*
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Peptide Fragments / chemistry*
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Peptides / chemical synthesis
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Peptides / chemistry
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Peptides / pharmacology*
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Phenyl Ethers / chemistry
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Stereoisomerism
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Structure-Activity Relationship
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Time Factors
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Xylenes / chemistry
Substances
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Amyloid beta-Peptides
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Aniline Compounds
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Benzamides
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Caffeic Acids
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Peptide Fragments
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Peptides
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Phenyl Ethers
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Xylenes
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amyloid beta-protein (1-40)
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1,3-xylenediamine
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phenylethyl 3-methylcaffeate
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Glycine