Publication | Open Access
Cholesterol <i>seco</i>‐Sterol‐Induced Aggregation of Methylated Amyloid‐β Peptides—Insights into Aldehyde‐Initiated Fibrillization of Amyloid‐β
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2008
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Proteinlipid InteractionMolecular BiologyPeptide ScienceProtein Phase SeparationAnalytical UltracentrifugationHot SpotLys 16Central Hydrophobic ClusterProtein FoldingProtein MisfoldingProtein FunctionOxysterolBiochemistryMethylated Amyloid‐β Peptides—insightsAldehyde‐initiated FibrillizationLipid ScienceBiomolecular EngineeringNatural SciencesLipid ChemistryMedicineLysosomal Storage Disease
Hot spot on amyloid-β? Atheronal-B-induced aggregation of amyloid-β (Aβ) involves a site-specific adduction of the aldehyde to the ε-amino group of Lys 16, suggesting that Lys 16 is a hot spot for atheronal-induced fibrillization of Aβ (see scheme). This process can be inhibited by molecules like cholesterol that compete for the central hydrophobic cluster binding domain. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2008/z705922_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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