000140001 001__ 140001
000140001 005__ 20210129212738.0
000140001 0247_ $$2WOS$$aWOS:000327285100013
000140001 0247_ $$2DOI$$a10.1016/j.bpj.2013.09.045
000140001 0247_ $$2altmetric$$aaltmetric:1999139
000140001 0247_ $$2pmid$$apmid:24268144
000140001 037__ $$aFZJ-2013-05968
000140001 041__ $$aEnglish
000140001 082__ $$a570
000140001 1001_ $$0P:(DE-Juel1)140589$$aPoojari, Chetan$$b0$$ufzj
000140001 245__ $$aMembrane Permeation Induced by Aggregates of Human Islet Amyloid Polypeptides
000140001 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2013
000140001 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1385652221_8463
000140001 3367_ $$2DataCite$$aOutput Types/Journal article
000140001 3367_ $$00$$2EndNote$$aJournal Article
000140001 3367_ $$2BibTeX$$aARTICLE
000140001 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000140001 3367_ $$2DRIVER$$aarticle
000140001 500__ $$3POF3_Assignment on 2016-02-29
000140001 520__ $$aSeveral neurodegenerative diseases such as Alzheimer’s and Parkinson’s diseases as well as nonneuropathic diseases such as type II diabetes and atrial amyloidosis are associated with aggregation of amyloid polypeptides into fibrillar structures, or plaques. In this study, we use molecular dynamics simulations to test the stability and orientation of membrane-embedded aggregates of the human islet amyloid polypeptide (hIAPP) implicated in type II diabetes. We find that in both monolayers and bilayers of dipalmitoylphosphatidylglycerol (DPPG) hIAPP trimers and tetramers remain inside the membranes and preserve their β-sheet secondary structure. Lipid bilayer-inserted hIAPP trimers and tetramers orient inside DPPG at 60° relative to the membrane/water interface and lead to water permeation and Na+ intrusion, consistent with ion-toxicity in islet β-cells. In particular, hIAPP trimers form a water-filled β-sandwich that induce water permeability comparable with channel-forming proteins, such as aquaporins and gramicidin-A. The predicted disruptive orientation is consistent with the amphiphilic properties of the hIAPP aggregates and could be probed by chiral sum frequency generation (SFG) spectroscopy, as predicted by the simulated SFG spectra.
000140001 536__ $$0G:(DE-HGF)POF2-452$$a452 - Structural Biology (POF2-452)$$cPOF2-452$$fPOF II$$x0
000140001 7001_ $$0P:(DE-HGF)0$$aXiao, D.$$b1
000140001 7001_ $$0P:(DE-HGF)0$$aBatista, V. S.$$b2
000140001 7001_ $$0P:(DE-Juel1)132024$$aStrodel, Birgit$$b3$$eCorresponding author$$ufzj
000140001 773__ $$0PERI:(DE-600)1477214-0$$a10.1016/j.bpj.2013.09.045$$p2323-2332$$tBiophysical journal$$v105$$x0006-3495
000140001 8564_ $$uhttp://www.sciencedirect.com/science/article/pii/S000634951301120X#
000140001 8564_ $$uhttps://juser.fz-juelich.de/record/140001/files/FZJ-2013-05968.pdf$$yRestricted
000140001 909CO $$ooai:juser.fz-juelich.de:140001$$pVDB
000140001 9141_ $$y2013
000140001 915__ $$0StatID:(DE-HGF)0010$$2StatID$$aJCR/ISI refereed
000140001 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR
000140001 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000140001 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000140001 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000140001 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000140001 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000140001 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000140001 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000140001 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000140001 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000140001 9101_ $$0I:(DE-Juel1)ICS-6-20110106$$6P:(DE-Juel1)140589$$aStrukturbiochemie $$b0$$kICS-6
000140001 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)140589$$aForschungszentrum Jülich GmbH$$b0$$kFZJ
000140001 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132024$$aForschungszentrum Jülich GmbH$$b3$$kFZJ
000140001 9132_ $$0G:(DE-HGF)POF3-559H$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vAddenda$$x0
000140001 9131_ $$0G:(DE-HGF)POF2-452$$1G:(DE-HGF)POF2-450$$2G:(DE-HGF)POF2-400$$3G:(DE-HGF)POF2$$4G:(DE-HGF)POF$$aDE-HGF$$bSchlüsseltechnologien$$lBioSoft$$vStructural Biology$$x0
000140001 920__ $$lyes
000140001 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$kICS-6$$lStrukturbiochemie $$x0
000140001 980__ $$ajournal
000140001 980__ $$aVDB
000140001 980__ $$aUNRESTRICTED
000140001 980__ $$aI:(DE-Juel1)ICS-6-20110106
000140001 981__ $$aI:(DE-Juel1)IBI-7-20200312