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| 001 | 858908 | ||
| 005 | 20210130000132.0 | ||
| 024 | 7 | _ | |a 10.1021/acschemneuro.8b00065 |2 doi |
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| 082 | _ | _ | |a 540 |
| 100 | 1 | _ | |a Österlund, Nicklas |0 0000-0003-0905-7911 |b 0 |
| 245 | _ | _ | |a Amyloid-β Peptide Interactions with Amphiphilic Surfactants: Electrostatic and Hydrophobic Effects |
| 260 | _ | _ | |a Washington, DC |c 2018 |b ACS Publ. |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a The amphiphilic nature of the amyloid-β (Aβ) peptide associated with Alzheimer's disease facilitates various interactions with biomolecules such as lipids and proteins, with effects on both structure and toxicity of the peptide. Here, we investigate these peptide-amphiphile interactions by experimental and computational studies of Aβ(1-40) in the presence of surfactants with varying physicochemical properties. Our findings indicate that electrostatic peptide-surfactant interactions are required for coclustering and structure induction in the peptide and that the strength of the interaction depends on the surfactant net charge. Both aggregation-prone peptide-rich coclusters and stable surfactant-rich coclusters can form. Only Aβ(1-40) monomers, but not oligomers, are inserted into surfactant micelles in this surfactant-rich state. Surfactant headgroup charge is suggested to be important as electrostatic peptide-surfactant interactions on the micellar surface seems to be an initiating step toward insertion. Thus, no peptide insertion or change in peptide secondary structure is observed using a nonionic surfactant. The hydrophobic peptide-surfactant interactions instead stabilize the Aβ monomer, possibly by preventing self-interaction between the peptide core and C-terminus, thereby effectively inhibiting the peptide aggregation process. These findings give increased understanding regarding the molecular driving forces for Aβ aggregation and the peptide interaction with amphiphilic biomolecules. |
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| 700 | 1 | _ | |a Kulkarni, Yashraj S. |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Misiaszek, Agata D. |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Wallin, Cecilia |0 0000-0003-4464-1769 |b 3 |
| 700 | 1 | _ | |a Krüger, Dennis M. |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Liao, Qinghua |0 P:(DE-HGF)0 |b 5 |
| 700 | 1 | _ | |a Mashayekhy Rad, Farshid |0 P:(DE-HGF)0 |b 6 |
| 700 | 1 | _ | |a Jarvet, Jüri |0 P:(DE-HGF)0 |b 7 |
| 700 | 1 | _ | |a Strodel, Birgit |0 P:(DE-Juel1)132024 |b 8 |
| 700 | 1 | _ | |a Wärmländer, Sebastian K. T. S. |0 0000-0001-6836-5610 |b 9 |
| 700 | 1 | _ | |a Ilag, Leopold L. |0 P:(DE-HGF)0 |b 10 |
| 700 | 1 | _ | |a Kamerlin, Shina C. L. |0 0000-0002-3190-1173 |b 11 |e Corresponding author |
| 700 | 1 | _ | |a Gräslund, Astrid |0 P:(DE-HGF)0 |b 12 |e Corresponding author |
| 773 | _ | _ | |a 10.1021/acschemneuro.8b00065 |g Vol. 9, no. 7, p. 1680 - 1692 |0 PERI:(DE-600)2528493-9 |n 7 |p 1680 - 1692 |t ACS chemical neuroscience |v 9 |y 2018 |x 1948-7193 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/858908/files/acschemneuro.8b00065.pdf |y Restricted |
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