An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils.


Journal

eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614

Informations de publication

Date de publication:
21 08 2019
Historique:
received: 25 02 2019
accepted: 04 08 2019
pubmed: 8 8 2019
medline: 12 2 2020
entrez: 8 8 2019
Statut: epublish

Résumé

Removing or preventing the formation of [Formula: see text]-synuclein aggregates is a plausible strategy against Parkinson's disease. To this end, we have engineered the [Formula: see text]-wrapin AS69 to bind monomeric [Formula: see text]-synuclein with high affinity. In cultured cells, AS69 reduced the self-interaction of [Formula: see text]-synuclein and formation of visible [Formula: see text]-synuclein aggregates. In flies, AS69 reduced [Formula: see text]-synuclein aggregates and the locomotor deficit resulting from [Formula: see text]-synuclein expression in neuronal cells. In biophysical experiments in vitro, AS69 highly sub-stoichiometrically inhibited both primary and autocatalytic secondary nucleation processes, even in the presence of a large excess of monomer. We present evidence that the AS69-[Formula: see text]-synuclein complex, rather than the free AS69, is the inhibitory species responsible for sub-stoichiometric inhibition of secondary nucleation. These results represent a new paradigm that high affinity monomer binders can lead to strongly sub-stoichiometric inhibition of nucleation processes.

Identifiants

pubmed: 31389332
doi: 10.7554/eLife.46112
pii: 46112
pmc: PMC6721797
doi:
pii:

Substances chimiques

Amyloid 0
Recombinant Proteins 0
alpha-Synuclein 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : H2020 European Research Council
ID : 726368
Pays : International
Organisme : H2020 Marie Skłodowska-Curie Actions
ID : 706551
Pays : International
Organisme : RWTH Aachen University
ID : START-Program of the Faculty of Medicine
Pays : International
Organisme : H2020 European Research Council
ID : MCSA grant agreement No 706551
Pays : International
Organisme : European Commission
ID : 706551
Pays : International

Informations de copyright

© 2019, Agerschou et al.

Déclaration de conflit d'intérêts

EA, PF, TS, CG, DK, LH, VP, HS, DW, CD, AV, BF, WH, AB No competing interests declared

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Auteurs

Emil Dandanell Agerschou (ED)

Institut für Physikalische Biologie, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.

Patrick Flagmeier (P)

Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.
Centre for Misfolding Diseases, University of Cambridge, Cambridge, United Kingdom.

Theodora Saridaki (T)

Department of Neurology, RWTH Aachen University, Aachen, Germany.

Céline Galvagnion (C)

RG Mechanisms of Neuroprotection, German Centre for Neurodegenerative Diseases (DZNE), Bonn, Germany.
Department of Pharmacology and Drug Design, University of Copenhagen, Copenhagen, Denmark.

Daniel Komnig (D)

Department of Neurology, RWTH Aachen University, Aachen, Germany.

Laetitia Heid (L)

Institut für Physikalische Biologie, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.

Vibha Prasad (V)

Department of Neurology, RWTH Aachen University, Aachen, Germany.

Hamed Shaykhalishahi (H)

Institut für Physikalische Biologie, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.

Dieter Willbold (D)

Institut für Physikalische Biologie, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
Institute of Complex Systems (ICS-6), Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.

Christopher M Dobson (CM)

Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.
Centre for Misfolding Diseases, University of Cambridge, Cambridge, United Kingdom.

Aaron Voigt (A)

Department of Neurology, RWTH Aachen University, Aachen, Germany.

Bjoern Falkenburger (B)

Department of Neurology, RWTH Aachen University, Aachen, Germany.
Department of Neurology, Dresden University Medical Center, Dresden, Germany.
JARA BRAIN Institute II, Julich and Aachen, Germany.

Wolfgang Hoyer (W)

Institut für Physikalische Biologie, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
Institute of Complex Systems (ICS-6), Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany.

Alexander K Buell (AK)

Institut für Physikalische Biologie, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
Department of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, Denmark.

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Classifications MeSH