Authors: Oliva, Rosario
Mukherjee, Sanjib K.
Ostermeier, Lena
Pazurek, Lilli A.
Kriegler, Simon
Bader, Verian
Prumbaum, Daniel
Raunser, Stefan
Winklhofer, Konstanze F.
Tatzelt, Jörg
Winter, Roland
Title: Remodeling of the fibrillation pathway of α-synuclein by interaction with antimicrobial peptide LL-III
Language (ISO): en
Abstract: 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 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.
Subject Headings: α-synuclein
Antimicrobial peptide
Lewy bodies
Liquid-liquid phase separation
Protein condensate
Issue Date: 2021-06-24
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Appears in Collections:Physikalische Chemie

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