| Literature DB >> 25179684 |
Erika Sironi1, Laura Colombo, Angela Lompo, Massimo Messa, Marcella Bonanomi, Maria Elena Regonesi, Mario Salmona, Cristina Airoldi.
Abstract
By combining NMR spectroscopy, transmission electron microscopy, and circular dichroism we have identified the structural determinants involved in the interaction of green tea catechins with Aβ1-42, PrP106-126, and ataxin-3 oligomers. The data allow the elucidation of their mechanism of action, showing that the flavan-3-ol unit of catechins is essential for interaction. At the same time, the gallate moiety, when present, seems to increase the affinity for the target proteins. These results provide important information for the rational design of new compounds with anti-amyloidogenic activity and/or molecular tools for the specific targeting of amyloid aggregates in vivo.Entities:
Keywords: NMR spectroscopy; amyloid peptides; circular dichroism; molecular recognition; structure-activity relationship
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Year: 2014 PMID: 25179684 DOI: 10.1002/chem.201403188
Source DB: PubMed Journal: Chemistry ISSN: 0947-6539 Impact factor: 5.236