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Current Pharmaceutical Design


ISSN (Print): 1381-6128
ISSN (Online): 1873-4286

Inhibition of Protein Misfolding and Aggregation by Small Rationally-Designed Peptides

Author(s): L. D. Estrada and C. Soto

Volume 12, Issue 20, 2006

Page: [2557 - 2567] Pages: 11

DOI: 10.2174/138161206777698792

Price: $65


Several human diseases are associated with the presence of toxic fibrillar protein deposits. These diseases called protein misfolding disorders, are characterized by the accumulation of misfolded protein aggregates in diverse tissues. Strong evidence indicates that the conversion of a normal soluble protein into a β-sheet-rich oligomeric structure and further fibrillar aggregation are the key events in the disease pathogenesis. Therefore, a promising therapeutic target consists of the prevention and dissolution of misfolded protein aggregates. Peptides designed to specifically bind to the pathogenic protein and block and/or reverse its abnormal conformational change constitute a new class of drugs. This article reviews this approach, describing diverse compounds reported to have this activity.

Keywords: Peptide inhibitors, β-sheet breakers, amyloid, conformational disorders, Alzheimer's disease

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