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Article

Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation

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Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Universidad de Zaragoza, Pedro Cerbuna 12, 50009 Zaragoza, Spain
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Biocomputation and Complex Systems Physics Institute (BIFI), Joint Unit BIFI-IQFR (CSIC), Mariano Esquillor s/n, Edificio I + D, 50018 Zaragoza, Spain
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Institut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spain
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Aragon Health Research Institute (IIS Aragón), Universidad de Zaragoza, 50009 Zaragoza, Spain
*
Authors to whom correspondence should be addressed.
Academic Editor: Masatoshi Maki
Int. J. Mol. Sci. 2016, 17(6), 964; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms17060964
Received: 11 January 2016 / Revised: 8 June 2016 / Accepted: 13 June 2016 / Published: 18 June 2016
(This article belongs to the Collection Protein Folding)
Human Amylin, or islet amyloid polypeptide (hIAPP), is a small hormone secreted by pancreatic β-cells that forms aggregates under insulin deficiency metabolic conditions, and it constitutes a pathological hallmark of type II diabetes mellitus. In type II diabetes patients, amylin is abnormally increased, self-assembled into amyloid aggregates, and ultimately contributes to the apoptotic death of β-cells by mechanisms that are not completely understood. We have screened a library of approved drugs in order to identify inhibitors of amylin aggregation that could be used as tools to investigate the role of amylin aggregation in type II diabetes or as therapeutics in order to reduce β-cell damage. Interestingly, three of the compounds analyzed—benzbromarone, quercetin, and folic acid—are able to slow down amylin fiber formation according to Thioflavin T binding, turbidimetry, and Transmission Electron Microscopy assays. In addition to the in vitro assays, we have tested the effect of these compounds in an amyloid toxicity cell culture model and we have found that one of them, quercetin, has the ability to partly protect cultured pancreatic insulinoma cells from the cytotoxic effect of amylin. Our data suggests that quercetin can contribute to reduce oxidative damage in pancreatic insulinoma β cells by modulating the aggregation propensity of amylin. View Full-Text
Keywords: quercetin; benzbromarone; folic acid; amylin; amyloid; aggregation; type II diabetes quercetin; benzbromarone; folic acid; amylin; amyloid; aggregation; type II diabetes
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MDPI and ACS Style

López, L.C.; Varea, O.; Navarro, S.; Carrodeguas, J.A.; Sanchez de Groot, N.; Ventura, S.; Sancho, J. Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation. Int. J. Mol. Sci. 2016, 17, 964. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms17060964

AMA Style

López LC, Varea O, Navarro S, Carrodeguas JA, Sanchez de Groot N, Ventura S, Sancho J. Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation. International Journal of Molecular Sciences. 2016; 17(6):964. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms17060964

Chicago/Turabian Style

López, Laura C., Olga Varea, Susanna Navarro, José A. Carrodeguas, Natalia Sanchez de Groot, Salvador Ventura, and Javier Sancho. 2016. "Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation" International Journal of Molecular Sciences 17, no. 6: 964. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms17060964

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