Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 20, Issue 42, Pages 13793-13800Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201403188
Keywords
amyloid peptides; circular dichroism; molecular recognition; structure-activity relationship; NMR spectroscopy
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Funding
- Regione Lombardia
- Fondo per la Promozione di Accordi Istituzionali [4779]
- Banca IntesaSanpaolo Grant
- CINMPIS (Consorzio Interuniversitario Nazionale di ricerca in Metodologie e Processi Innovativi di Sintesi)
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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 A1-42, 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.
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