Journal
CHEMMEDCHEM
Volume 2, Issue 12, Pages 1674-1692Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cmdc.200700140
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Funding
- NIAID NIH HHS [R01AI68414] Funding Source: Medline
- NIA NIH HHS [R21AG025954] Funding Source: Medline
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The devastating effects of Alzheimer's and related omyloidogenic diseases hove 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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