Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism

By Y. Porat, A. Abramowitz, Ehud Gazit. Chemical Biology and Drug Design, 2006

973 citations recorded by the source corpus.

Subfields: Biomaterials, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/8c1e8b94fc05b6f49418a65253af08846e66634a

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In Molecular Biology

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Citations in the corpus

• EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers (2008, background): “EGCG is an aromatic compound with a large number of hydroxyl groups [ 46 ], suggesting that it might induce intermolecular interactions between αS monomers that are stabilized by hydrogen bonds involving the hydroxyl groups.”
• Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils (2010, background): “Similar compounds such as Congo red have to varying degrees displayed a capacity to both enhance and inhibit fibril formation [65,66], potentially compromising their objectivity as diagnostic tools.”