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| Hauptseite > Publikationsdatenbank > Direct disassembly of α-syn preformed fibrils into α-syn monomers by an all-D-peptide > print |
| Hauptseite > Publikationsdatenbank > Direct disassembly of α-syn preformed fibrils into α-syn monomers by an all-D-peptide > print |
| 001 | 1046551 | ||
| 005 | 20250930132709.0 | ||
| 024 | 7 | _ | |a 10.1038/s41531-025-01132-7 |2 doi |
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| 100 | 1 | _ | |a Sevenich, Marc |0 P:(DE-Juel1)165152 |b 0 |
| 245 | _ | _ | |a Direct disassembly of α-syn preformed fibrils into α-syn monomers by an all-D-peptide |
| 260 | _ | _ | |a [London] |c 2025 |b Springer Nature |
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| 520 | _ | _ | |a A hallmark of Parkinson's disease (PD) is the progressive neurodegeneration associated with soluble oligomeric and fibrillar forms of misfolded α-synuclein (α-syn). In this study, all-D-enantiomeric peptide ligands are presented that bind monomeric α-syn with high affinity, stabilize its physiological monomeric status, prevent aggregation and dissolve existing aggregates. This "antiprionic" mode of action directly targets pathogenic aggregated particles. Using mirror-image phage display on D-enantiomeric full-length α-syn, SVD-1 and SVD-1a were identified, showing a delay of aggregation and reduction of aggregate formation in both de novo and seeded models. Picomolar KDs were confirmed by SPR, where a highly dynamic interaction mode was verified by PRE-NMR. SVD-1a also reduced the toxicity and intracellular seeding of α-syn fibrils in cell culture by disassembling them into monomers, as confirmed by atomic force microscopy and dynamic light scattering. These results support SVD-1a as a promising lead compound for the treatment of Parkinson's disease. |
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| 773 | _ | _ | |a 10.1038/s41531-025-01132-7 |g Vol. 11, no. 1, p. 271 |0 PERI:(DE-600)2819218-7 |n 1 |p 271 |t npj Parkinson's Disease |v 11 |y 2025 |x 2373-8057 |
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