Remodeling of the fibrillation pathway of α-synuclein by interaction with antimicrobial peptide LL-III

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dc.contributor.authorOliva, Rosario
dc.contributor.authorMukherjee, Sanjib K.
dc.contributor.authorOstermeier, Lena
dc.contributor.authorPazurek, Lilli A.
dc.contributor.authorKriegler, Simon
dc.contributor.authorBader, Verian
dc.contributor.authorPrumbaum, Daniel
dc.contributor.authorRaunser, Stefan
dc.contributor.authorWinklhofer, Konstanze F.
dc.contributor.authorTatzelt, Jörg
dc.contributor.authorWinter, Roland
dc.date.accessioned2022-03-23T14:04:19Z
dc.date.available2022-03-23T14:04:19Z
dc.date.issued2021-06-24
dc.description.abstractLiquid-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 α-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 α-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 α-synuclein will contribute to the understanding of disease mechanisms (that arise in such condensates) and may also open up exciting new avenues for intervention.en
dc.identifier.urihttp://hdl.handle.net/2003/40820
dc.identifier.urihttp://dx.doi.org/10.17877/DE290R-22677
dc.language.isoende
dc.relation.ispartofseriesChemistry - a European journal;27(46)
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectα-synucleinen
dc.subjectAntimicrobial peptideen
dc.subjectLewy bodiesen
dc.subjectLiquid-liquid phase separationen
dc.subjectLL-IIIen
dc.subjectProtein condensateen
dc.subject.ddc540
dc.titleRemodeling of the fibrillation pathway of α-synuclein by interaction with antimicrobial peptide LL-IIIen
dc.typeTextde
dc.type.publicationtypearticlede
dcterms.accessRightsopen access
eldorado.secondarypublicationtruede
eldorado.secondarypublication.primarycitationR. Oliva, S. K. Mukherjee, L. Ostermeier, L. A. Pazurek, S. Kriegler, V. Bader, D. Prumbaum, S. Raunser, K. F. Winklhofer, J. Tatzelt, R. Winter, Chem. Eur. J. 2021, 27, 11845.de
eldorado.secondarypublication.primaryidentifierhttps://doi.org/10.1002/chem.202101592de

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