Abstract
Herein we report that a preferable inhibition of the nucleation phase of Aβ42, related to the formation of toxic oligomers, by triterpenoids from medicinal herbs originates from a salt bridge of their carboxy groups with Lys16 and 28 in Aβ42. Such a direct interaction targeting the monomer, dimer, and trimer suppressed further oligomerization. In contrast, the corresponding congeners without carboxy groups failed to do so.
MeSH terms
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Amyloid beta-Peptides / chemistry*
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Anthraquinones / chemistry
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Anthraquinones / pharmacology
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Carboxylic Acids / chemistry
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Carboxylic Acids / pharmacology*
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Cell Line, Tumor
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Humans
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Lysine / chemistry
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Neuroprotective Agents / chemistry
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Neuroprotective Agents / pharmacology*
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Oleanolic Acid / analogs & derivatives*
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Oleanolic Acid / chemistry
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Oleanolic Acid / pharmacology*
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Pentacyclic Triterpenes / chemistry
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Pentacyclic Triterpenes / pharmacology
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Peptide Fragments / chemistry*
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Protein Multimerization
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Triterpenes / chemistry
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Triterpenes / pharmacology
Substances
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Amyloid beta-Peptides
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Anthraquinones
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Carboxylic Acids
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Neuroprotective Agents
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Pentacyclic Triterpenes
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Peptide Fragments
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Triterpenes
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amyloid beta-protein (1-42)
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uncarinic acid-C
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Oleanolic Acid
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asiatic acid
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Lysine
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rhein