Catechol-Containing Hydroxylated Biomimetic 4-Thiaflavanes as Inhibitors of Amyloid Aggregation
AbstractThe 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
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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.
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(2):6.Chicago/Turabian Style
Ramazzotti, Matteo; Paoli, Paolo; Tiribilli, Bruno; Viglianisi, Caterina; Menichetti, Stefano; Degl’innocenti, Donatella. 2017. "Catechol-Containing Hydroxylated Biomimetic 4-Thiaflavanes as Inhibitors of Amyloid Aggregation." Biomimetics 2, no. 2: 6.
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