000056165 001__ 56165 000056165 005__ 20200221144312.0 000056165 0247_ $$2doi$$a10.3390/ijms17060964 000056165 0248_ $$2sideral$$a95298 000056165 037__ $$aART-2016-95298 000056165 041__ $$aeng 000056165 100__ $$aLópez, L.C. 000056165 245__ $$aBenzbromarone, quercetin, and folic acid inhibit amylin aggregation 000056165 260__ $$c2016 000056165 5060_ $$aAccess copy available to the general public$$fUnrestricted 000056165 5203_ $$aHuman Amylin, or islet amyloid polypeptide (hIAPP), is a small hormone secreted by pancreatic ß-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 ß-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 ß-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 ß cells by modulating the aggregation propensity of amylin. 000056165 536__ $$9info:eu-repo/grantAgreement/ES/MICINN/BFU2013-44763-P$$9info:eu-repo/grantAgreement/ES/MINECO/BFU2013-47064-P$$9info:eu-repo/grantAgreement/ES/UZ/UZ2011-BIO-02 000056165 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/ 000056165 590__ $$a3.226$$b2016 000056165 591__ $$aCHEMISTRY, MULTIDISCIPLINARY$$b54 / 166 = 0.325$$c2016$$dQ2$$eT1 000056165 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b116 / 287 = 0.404$$c2016$$dQ2$$eT2 000056165 592__ $$a1.235$$b2016 000056165 593__ $$aMedicine (miscellaneous)$$c2016$$dQ1 000056165 593__ $$aPhysical and Theoretical Chemistry$$c2016$$dQ1 000056165 593__ $$aComputer Science Applications$$c2016$$dQ1 000056165 593__ $$aInorganic Chemistry$$c2016$$dQ1 000056165 593__ $$aSpectroscopy$$c2016$$dQ1 000056165 593__ $$aOrganic Chemistry$$c2016$$dQ1 000056165 593__ $$aMolecular Biology$$c2016$$dQ2 000056165 593__ $$aCatalysis$$c2016$$dQ2 000056165 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion 000056165 700__ $$aVarea, O. 000056165 700__ $$aNavarro, S. 000056165 700__ $$0(orcid)0000-0003-0062-1029$$aCarrodeguas, J.A.$$uUniversidad de Zaragoza 000056165 700__ $$aDe Groot, N.S. 000056165 700__ $$aVentura, S. 000056165 700__ $$0(orcid)0000-0002-2879-9200$$aSancho, J.$$uUniversidad de Zaragoza 000056165 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole. 000056165 773__ $$g17, 6 (2016), 964 [12 pp]$$pInt. j. mol. sci.$$tInternational Journal of Molecular Sciences$$x1661-6596 000056165 8564_ $$s2215331$$uhttps://zaguan.unizar.es/record/56165/files/texto_completo.pdf$$yVersión publicada 000056165 8564_ $$s105516$$uhttps://zaguan.unizar.es/record/56165/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada 000056165 909CO $$ooai:zaguan.unizar.es:56165$$particulos$$pdriver 000056165 951__ $$a2020-02-21-13:37:36 000056165 980__ $$aARTICLE