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Harnessing Chaperones to Generate Small-Molecule Inhibitors of Amyloid β Aggregation
Jason E. Gestwicki, Gerald R. Crabtree and Isabella A. Graef
New Series, Vol. 306, No. 5697 (Oct. 29, 2004), pp. 865-869
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/3839541
Page Count: 5
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Protein aggregation is involved in the pathogenesis of neurodegenerative diseases and hence is considered an attractive target for therapeutic intervention. However, protein-protein interactions are exceedingly difficult to inhibit. Small molecules lack sufficient steric bulk to prevent interactions between large peptide surfaces. To yield potent inhibitors of β-amyloid (Aβ) aggregation, we synthesized small molecules that increase their steric bulk by binding to chaperones but also have a moiety available for interaction with Aβ. This strategy yields potent inhibitors of Aβ aggregation and could lead to therapeutics for Alzheimer's disease and other forms of neurodegeneration.
Science © 2004 American Association for the Advancement of Science