flavan-3-ol and Protein-Aggregation--Pathological

flavan-3-ol has been researched along with Protein-Aggregation--Pathological* in 1 studies

Other Studies

1 other study(ies) available for flavan-3-ol and Protein-Aggregation--Pathological

ArticleYear
Natural compounds against neurodegenerative diseases: molecular characterization of the interaction of catechins from green tea with Aβ1-42, PrP106-126, and ataxin-3 oligomers.
    Chemistry (Weinheim an der Bergstrasse, Germany), 2014, Oct-13, Volume: 20, Issue:42

    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.

    Topics: Amino Acid Sequence; Amyloid beta-Peptides; Ataxin-3; Biological Products; Catechin; Flavonoids; Humans; Molecular Sequence Data; Nerve Tissue Proteins; Neurodegenerative Diseases; Nuclear Magnetic Resonance, Biomolecular; Nuclear Proteins; Peptide Fragments; Prions; Protein Aggregation, Pathological; Repressor Proteins; Tea

2014