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| 001 | 279291 | ||
| 005 | 20220930130052.0 | ||
| 024 | 7 | _ | |a 10.1002/anie.201503018 |2 doi |
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| 100 | 1 | _ | |a Shaykhalishahi, Hamed |0 P:(DE-Juel1)167315 |b 0 |u fzj |
| 245 | _ | _ | |a Contact between the β1 and β2 Segments of α-Synuclein that Inhibits Amyloid Formation |
| 260 | _ | _ | |a Weinheim |c 2015 |b Wiley-VCH |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1449667650_32511 |2 PUB:(DE-HGF) |
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| 520 | _ | _ | |a Conversion of the intrinsically disordered protein α-synuclein (α-syn) into amyloid aggregates is a key process in Parkinson’s disease. The sequence region 35–59 contains β-strand segments β1 and β2 of α-syn amyloid fibril models and most disease-related mutations. β1 and β2 frequently engage in transient interactions in monomeric α-syn. The consequences of β1–β2 contacts are evaluated by disulfide engineering, biophysical techniques, and cell viability assays. The double-cysteine mutant α-synCC, with a disulfide linking β1 and β2, is aggregation-incompetent and inhibits aggregation and toxicity of wild-type α-syn. We show that α-syn delays the aggregation of amyloid-β peptide and islet amyloid polypeptide involved in Alzheimer’s disease and type 2 diabetes, an effect enhanced in the α-synCC mutant. Tertiary interactions in the β1–β2 region of α-syn interfere with the nucleation of amyloid formation, suggesting promotion of such interactions as a potential therapeutic approach. |
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| 700 | 1 | _ | |a Gauhar, Aziz |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Wördehoff, Michael M. |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Grüning, Clara S. R. |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Klein, Antonia N. |0 P:(DE-Juel1)145785 |b 4 |u fzj |
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| 700 | 1 | _ | |a Hoyer, Wolfgang |0 P:(DE-Juel1)166306 |b 9 |e Corresponding author |u fzj |
| 773 | _ | _ | |a 10.1002/anie.201503018 |g Vol. 54, no. 30, p. 8837 - 8840 |0 PERI:(DE-600)2011836-3 |n 30 |p 8837 - 8840 |t Angewandte Chemie / International edition |v 54 |y 2015 |x 1433-7851 |
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