guest ::
| Home > Publications database > Membrane Permeation Induced by Aggregates of Human Islet Amyloid Polypeptides > print |
| Home > Publications database > Membrane Permeation Induced by Aggregates of Human Islet Amyloid Polypeptides > print |
| 001 | 140001 | ||
| 005 | 20210129212738.0 | ||
| 024 | 7 | _ | |a WOS:000327285100013 |2 WOS |
| 024 | 7 | _ | |a 10.1016/j.bpj.2013.09.045 |2 DOI |
| 024 | 7 | _ | |a altmetric:1999139 |2 altmetric |
| 024 | 7 | _ | |a pmid:24268144 |2 pmid |
| 037 | _ | _ | |a FZJ-2013-05968 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Poojari, Chetan |0 P:(DE-Juel1)140589 |b 0 |u fzj |
| 245 | _ | _ | |a Membrane Permeation Induced by Aggregates of Human Islet Amyloid Polypeptides |
| 260 | _ | _ | |a New York, NY |c 2013 |b Rockefeller Univ. Press |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1385652221_8463 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 500 | _ | _ | |3 POF3_Assignment on 2016-02-29 |
| 520 | _ | _ | |a Several 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. |
| 536 | _ | _ | |a 452 - Structural Biology (POF2-452) |0 G:(DE-HGF)POF2-452 |c POF2-452 |x 0 |f POF II |
| 700 | 1 | _ | |a Xiao, D. |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Batista, V. S. |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Strodel, Birgit |0 P:(DE-Juel1)132024 |b 3 |u fzj |e Corresponding author |
| 773 | _ | _ | |0 PERI:(DE-600)1477214-0 |x 0006-3495 |t Biophysical journal |p 2323-2332 |v 105 |a 10.1016/j.bpj.2013.09.045 |
| 856 | 4 | _ | |u http://www.sciencedirect.com/science/article/pii/S000634951301120X# |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/140001/files/FZJ-2013-05968.pdf |y Restricted |
| 909 | C | O | |o oai:juser.fz-juelich.de:140001 |p VDB |
| 910 | 1 | _ | |a Strukturbiochemie |0 I:(DE-Juel1)ICS-6-20110106 |k ICS-6 |b 0 |6 P:(DE-Juel1)140589 |
| 910 | 1 | _ | |a Forschungszentrum Jülich GmbH |0 I:(DE-588b)5008462-8 |k FZJ |b 0 |6 P:(DE-Juel1)140589 |
| 910 | 1 | _ | |a Forschungszentrum Jülich GmbH |0 I:(DE-588b)5008462-8 |k FZJ |b 3 |6 P:(DE-Juel1)132024 |
| 913 | 2 | _ | |a DE-HGF |b Key Technologies |l BioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences |1 G:(DE-HGF)POF3-550 |0 G:(DE-HGF)POF3-559H |2 G:(DE-HGF)POF3-500 |v Addenda |x 0 |
| 913 | 1 | _ | |a DE-HGF |b Schlüsseltechnologien |1 G:(DE-HGF)POF2-450 |0 G:(DE-HGF)POF2-452 |2 G:(DE-HGF)POF2-400 |v Structural Biology |x 0 |4 G:(DE-HGF)POF |3 G:(DE-HGF)POF2 |l BioSoft |
| 914 | 1 | _ | |y 2013 |
| 915 | _ | _ | |a JCR/ISI refereed |0 StatID:(DE-HGF)0010 |2 StatID |
| 915 | _ | _ | |a JCR |0 StatID:(DE-HGF)0100 |2 StatID |
| 915 | _ | _ | |a WoS |0 StatID:(DE-HGF)0110 |2 StatID |b Science Citation Index |
| 915 | _ | _ | |a WoS |0 StatID:(DE-HGF)0111 |2 StatID |b Science Citation Index Expanded |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0150 |2 StatID |b Web of Science Core Collection |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0199 |2 StatID |b Thomson Reuters Master Journal List |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0200 |2 StatID |b SCOPUS |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0300 |2 StatID |b Medline |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0310 |2 StatID |b NCBI Molecular Biology Database |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1030 |2 StatID |b Current Contents - Life Sciences |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1050 |2 StatID |b BIOSIS Previews |
| 920 | _ | _ | |l yes |
| 920 | 1 | _ | |0 I:(DE-Juel1)ICS-6-20110106 |k ICS-6 |l Strukturbiochemie |x 0 |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|