guest ::
| Home > Publications database > Amyloid Aggregation Inhibitory Mechanism of Arginine-rich D-peptides > print |
| Home > Publications database > Amyloid Aggregation Inhibitory Mechanism of Arginine-rich D-peptides > print |
| 001 | 153348 | ||
| 005 | 20210129213727.0 | ||
| 024 | 7 | _ | |a WOS:000333274400005 |2 WOS |
| 037 | _ | _ | |a FZJ-2014-02980 |
| 082 | _ | _ | |a 540 |
| 100 | 1 | _ | |a Olubiyi, Olujide |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Amyloid Aggregation Inhibitory Mechanism of Arginine-rich D-peptides |
| 260 | _ | _ | |a Hilversum [u.a.] |c 2014 |b Bentham Science Publ. |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1399880344_4089 |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 | _ | _ | |a Campus-weite Veröffentlichung erwünschtD. Willbold und B. Strodel sind beide "Corresponding Authors". |
| 520 | _ | _ | |a It is widely believed that Alzheimer's disease pathogenesis is driven by the production and deposition of the amyloid-β peptide (Aβ) in the brain. In this study, we employ a combination of in silico and in vitro approaches to investigate the inhibitory properties of selected arginine-rich D-enantiomeric peptides (D-peptides) against amyloid aggregation. The D-peptides include D3, a 12-residue peptide with anti-amyloid potencies demonstrated in vitro and in vivo, RD2, a scrambled sequence of D3, as well as truncated RD2 variants. Using a global optimization method together with binding free energy calculations followed by molecular dynamics simulations, we perform a detailed analysis of D-peptide binding to Aβ monomer and a fibrillar Aβ structure. Results obtained from both molecular simulations and surface plasmon resonance experiments reveal a strong binding of D3 and RD2 to Aβ, leading to a significant reduction in the amount of β structures in both monomer and fibril, which was also demonstrated in Thioflavin T assays. The binding of the D-peptides to Aβ is driven by electrostatic interactions, mostly involving the D-arginine residues and Glu11, Glu22 and Asp23 of Aβ. Furthermore, we show that the anti-amyloid activities of the D-peptides depend on the length and sequence of the Dpeptide, its ability to form multiple weak hydrophobic interactions with Aβ, as well as the Aβ oligomer size. |
| 536 | _ | _ | |a 452 - Structural Biology (POF2-452) |0 G:(DE-HGF)POF2-452 |c POF2-452 |f POF II |x 0 |
| 700 | 1 | _ | |a Frenzel, Daniel |0 P:(DE-Juel1)145441 |b 1 |
| 700 | 1 | _ | |a Bartnik, Dirk |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Glück, Julian |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Brener, O. |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Nagel-Steger, Luitgard |0 P:(DE-Juel1)162443 |b 5 |
| 700 | 1 | _ | |a Funke, S. A. |0 P:(DE-HGF)0 |b 6 |
| 700 | 1 | _ | |a Willbold, Dieter |0 P:(DE-Juel1)132029 |b 7 |e Corresponding Author |
| 700 | 1 | _ | |a Strodel, Birgit |0 P:(DE-Juel1)132024 |b 8 |
| 773 | _ | _ | |0 PERI:(DE-600)2034240-8 |p 1448-1457 |t Current medicinal chemistry |v 21 |y 2014 |x 1875-533X |
| 856 | 4 | _ | |u http://www.ingentaconnect.com/content/ben/cmc/2014/00000021/00000012/art00005 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/153348/files/FZJ-2014-02980.pdf |y Restricted |
| 909 | C | O | |o oai:juser.fz-juelich.de:153348 |p VDB |
| 910 | 1 | _ | |a Forschungszentrum Jülich GmbH |0 I:(DE-588b)5008462-8 |k FZJ |b 1 |6 P:(DE-Juel1)145441 |
| 910 | 1 | _ | |a Forschungszentrum Jülich GmbH |0 I:(DE-588b)5008462-8 |k FZJ |b 5 |6 P:(DE-Juel1)162443 |
| 910 | 1 | _ | |a Forschungszentrum Jülich GmbH |0 I:(DE-588b)5008462-8 |k FZJ |b 7 |6 P:(DE-Juel1)132029 |
| 910 | 1 | _ | |a Forschungszentrum Jülich GmbH |0 I:(DE-588b)5008462-8 |k FZJ |b 8 |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)POF3-553 |2 G:(DE-HGF)POF3-500 |v Physical Basis of Diseases |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 2014 |
| 915 | _ | _ | |a Peer review unknown |0 StatID:(DE-HGF)0040 |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 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1120 |2 StatID |b BIOSIS Reviews Reports And Meetings |
| 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 I:(DE-Juel1)ICS-6-20110106 |
| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|