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dc.rights.licenseopenen_US
dc.contributor.authorELENBAAS, Barend O. W.
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorKHEMTEMOURIAN, Lucie
dc.contributor.authorKILLIAN, J. Antoinette
dc.contributor.authorSINNIGE, Tessa
dc.date.accessioned2023-04-26T13:24:55Z
dc.date.available2023-04-26T13:24:55Z
dc.date.issued2022-06-24
dc.identifier.issn0006-2960en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/173217
dc.description.abstractEnType II diabetes is characterized by the loss of pancreatic β-cells. This loss is thought to be a consequence of membrane disruption, caused by the aggregation of islet amyloid polypeptide (IAPP) into amyloid fibrils. However, the molecular mechanisms of IAPP aggregation in the presence of membranes have remained unclear. Here, we use kinetic analysis to elucidate the aggregation mechanism of IAPP in the presence of mixed zwitterionic and anionic lipid membranes. The results converge to a model in which aggregation on the membrane is strongly dominated by secondary nucleation, that is, the formation of new nuclei on the surface of existing fibrils. The critical nucleus consists of a single IAPP molecule, and anionic lipids catalyze both primary and secondary nucleation, but not elongation. The fact that anionic lipids promote secondary nucleation implies that these events take place at the interface between the membrane and existing fibrils, demonstrating that fibril growth occurs at least to some extent on the membrane surface. These new insights into the mechanism of IAPP aggregation on membranes may help to understand IAPP toxicity and will be important for the development of therapeutics to prevent β-cell death in type II diabetes.
dc.language.isoENen_US
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.title.enMembrane-Catalyzed Aggregation of Islet Amyloid Polypeptide Is Dominated by Secondary Nucleation
dc.title.alternativeBiochemistryen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1021/acs.biochem.2c00184en_US
dc.subject.halChimie/Matériauxen_US
bordeaux.journalBiochemistryen_US
bordeaux.page1465-1472en_US
bordeaux.volume61en_US
bordeaux.hal.laboratoriesCBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248en_US
bordeaux.issue14en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.exportfalse
dc.rights.ccCC BYen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biochemistry&rft.date=2022-06-24&rft.volume=61&rft.issue=14&rft.spage=1465-1472&rft.epage=1465-1472&rft.eissn=0006-2960&rft.issn=0006-2960&rft.au=ELENBAAS,%20Barend%20O.%20W.&KHEMTEMOURIAN,%20Lucie&KILLIAN,%20J.%20Antoinette&SINNIGE,%20Tessa&rft.genre=article


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