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Biomimetics 2017, 2(2), 6; doi:10.3390/biomimetics2020006

Catechol-Containing Hydroxylated Biomimetic 4-Thiaflavanes as Inhibitors of Amyloid Aggregation

Dipartimento di Scienze Biomediche, Sperimentali e Cliniche, Università degli Studi di Firenze, viale G.B. Morgagni 50, 50134 Firenze, Italy
Dipartimento di Chimica “Ugo Schiff”, Polo Scientifico e Tecnologico, Università degli Studi di Firenze, via della Lastruccia 3-13, 50019 Sesto Fiorentino, Firenze, Italy
Consiglio Nazionale delle Ricerche (CNR), Istituto dei Sistemi Complessi, Via Madonna del Piano, 10, 50019 Sesto Fiorentino, Firenze, Italy
Authors to whom correspondence should be addressed.
Academic Editor: Daniel Ruiz-Molina
Received: 22 February 2017 / Revised: 3 May 2017 / Accepted: 4 May 2017 / Published: 9 May 2017
(This article belongs to the Special Issue Bioinspired Catechol-based Systems: Chemistry and Applications)
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The study of compounds able to interfere in various ways with amyloid aggregation is of paramount importance in amyloid research. Molecules characterized by a 4-thiaflavane skeleton have received great attention in chemical, medicinal, and pharmaceutical research. Such molecules, especially polyhydroxylated 4-thiaflavanes, can be considered as structural mimickers of several natural polyphenols that have been previously demonstrated to bind and impair amyloid fibril formation. In this work, we tested five different 4-thiaflavanes on the hen egg-white lysozyme (HEWL) amyloid model for their potential anti-amyloid properties. By combining a thioflavin T assay, atomic force microscopy, and a cell toxicity assay, we demonstrated that such compounds can impair the formation of high-order amyloid aggregates and mature fibrils. Despite this, the tested 4-thiaflavanes, although non-toxic per se, are not able to prevent amyloid toxicity on human neuroblastoma cells. Rather, they proved to block early aggregates in a stable, toxic conformation. Accordingly, 4-thiaflavanes can be proposed for further studies aimed at identifying blocking agents for the study of toxicity mechanisms of amyloid aggregation. View Full-Text
Keywords: catechol; hydroxylated 4-thiaflavanes; inhibition; amyloid aggregation; hen egg white lysozyme; antioxidant activity catechol; hydroxylated 4-thiaflavanes; inhibition; amyloid aggregation; hen egg white lysozyme; antioxidant activity

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Ramazzotti, M.; Paoli, P.; Tiribilli, B.; Viglianisi, C.; Menichetti, S.; Degl’innocenti, D. Catechol-Containing Hydroxylated Biomimetic 4-Thiaflavanes as Inhibitors of Amyloid Aggregation. Biomimetics 2017, 2, 6.

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