Remodeling of the fibrillation pathway of ��-synuclein by interaction with antimicrobial peptide LL-III
| Autor: | Oliva, Rosario, Mukherjee, Sanjib K., Ostermeier, Lena, Pazurek, Lilli A., Kriegler, Simon, Bader, Verian, Prumbaum, Daniel, Raunser, Stefan, Winklhofer, Konstanze F., Tatzelt, J��rg, Winter, Roland |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: | |
| DOI: | 10.17877/de290r-22677 |
| Popis: | Liquid-liquid phase separation (LLPS) has emerged as a key mechanism for intracellular organization, and many recent studies have provided important insights into the role of LLPS in cell biology. There is also evidence that LLPS is associated with a variety of medical conditions, including neurodegenerative disorders. Pathological aggregation of ��-synuclein, which is causally linked to Parkinson's disease, can proceed via droplet condensation, which then gradually transitions to the amyloid state. We show that the antimicrobial peptide LL-III is able to interact with both monomers and condensates of ��-synuclein, leading to stabilization of the droplet and preventing conversion to the fibrillar state. The anti-aggregation activity of LL-III was also confirmed in a cellular model. We anticipate that studying the interaction of antimicrobial-type peptides with liquid condensates such as ��-synuclein will contribute to the understanding of disease mechanisms (that arise in such condensates) and may also open up exciting new avenues for intervention. Chemistry - a European journal;27(46) |
| Databáze: | OpenAIRE |
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