Abstract
The intrinsic haemolysis of an amyloid-β (Aβ) N-terminal targeting gramicidin S derivative was successfully dissociated from its Aβ oligomer-preventing activities via Ala-scanning-based regulation of molecular amphiphilicity. The representative analogue DGR-7 shows low toxicity but significant efficiency in preventing Aβ oligomers and reducing amyloid plaques in APP/PS1 transgenic AD mice.
MeSH terms
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Alzheimer Disease / drug therapy*
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Alzheimer Disease / metabolism
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Amyloid beta-Peptides / chemistry*
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Amyloid beta-Peptides / metabolism*
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Animals
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Dose-Response Relationship, Drug
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Gramicidin / adverse effects
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Gramicidin / chemistry
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Gramicidin / pharmacology*
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Hemolysis / drug effects*
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Mice
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Mice, Transgenic
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Molecular Conformation / drug effects
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PC12 Cells
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Plaque, Amyloid / drug therapy*
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Plaque, Amyloid / metabolism
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Rats
Substances
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Amyloid beta-Peptides
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Gramicidin