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The Challenge of Inhibiting Aβ Polymerization

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The discovery of small molecules that inhibit β-peptide and other amyloid fibril formation has been impeded by featureless structure-activity-relationships, low apparent efficacy of inhibition, and by the perception that protein-protein interactions are too diffuse to be proper medicinal chemistry targets. Atomic resolution structural information on the critical target species are lacking. Despite these difficulties, substoichiometric inhibitors of fibrillogenesis have been reported. By carefully defining assay systems and considering a spectrum of data from different types of measurements, medicinal chemistry can improve molecular structures and their measured effectiveness can be better understood. Compounds with good pharmacokinetic and toxicologic profiles that persist in the target tissue at useful concentrations may be as useful as would extremely high affinity inhibitors with less favorable biological properties.

Keywords: amyloid beta peptide; polymerization

Document Type: Review Article


Publication date: June 1, 2002

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  • Current Medicinal Chemistry covers all the latest and outstanding developments in medicinal chemistry and rational drug design. Each issue contains a series of timely in-depth reviews written by leaders in the field covering a range of the current topics in medicinal chemistry. Current Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments.

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