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

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

1
Dipartimento di Scienze Biomediche, Sperimentali e Cliniche, Università degli Studi di Firenze, viale G.B. Morgagni 50, 50134 Firenze, Italy
2
Dipartimento di Chimica “Ugo Schiff”, Polo Scientifico e Tecnologico, Università degli Studi di Firenze, via della Lastruccia 3-13, 50019 Sesto Fiorentino, Firenze, Italy
3
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)
View Full-Text   |   Download PDF [4174 KB, uploaded 13 May 2017]   |  

Abstract

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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MDPI and ACS Style

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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