Many medical disorders are associated with amyloid formation, Alzheimer disease (AD) and Parkinson disease (PD) being perhaps the most well-known. All such diseases have in common the pathological aggregation of a normally soluble polypeptide chain into a series of oligomeric intermediates and ultimately into insoluble amyloid fibrils that accumulate within specific organs and tissues. The polyphenol (−)-epigallocatechin gallate (EGCG), extracted from green tea, is amongst the most promising small molecules with therapeutic potential to interfere with the pathogenic aggregation of amyloidogenic peptides and redirect their self-association into nontoxic assemblies. Investigation of the complexes formed by EGCG and amyloidogenic peptides has thus become the focus of many studies, in some cases producing apparently contradictory results. Two recent studies are briefly examined here in the light of results of other researchers.
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Contributed by Susan J. Tzotzos
Susan Tzotzos works for the Vienna-based biotech company Apeptico Forschung & Entwicklung GmbH, where she designs therapeutic peptides, oversees their synthesis and follows up their application in clinical trials. Susan also manages various research collaborations with university departments carrying out projects investigating the mode of action of Apeptico’s therapeutic peptides.