Published Research - Department of Chemistry

 

ORCID IDs

Cliff I. Stains

Date of this Version

12-2007

Comments

Published in ChemMedChem 2:12 (December 10, 2007), pp. 1674–1692; doi: 10.1002/cmdc.200700140 Copyright © 2007 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Used by permission.

Abstract

The devastating effects of Alzheimer’s and related amyloidogenic diseases have inspired the synthesis and evaluation of numerous ligands to understand the molecular mechanism of the aggregation of the beta-amyloid peptide. Our review focuses on the current knowledge in this field with respect to molecules that have been demonstrated to interact with either oligomeric or fibrillar forms of the beta-amyloid peptide. We describe natural proteins, peptides, peptidomimetics, and small molecules that have been found to interfere with beta-amyloid aggregation. We also detail recent efforts in selecting molecules that target beta-amyloid isolated from antibody, protein, and peptide libraries. These new molecules will likely aid in deciphering the details of the aggregation pathway for the beta-amyloid peptide and provide reagents that may stabilize relevant oligomeric intermediates which likely have bearing on the pathophysiology of Alzheimer’s disease. Moreover, the described anti-amyloid molecular toolbox will also provide an avenue for designing new diagnostic and therapeutic reagents.

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