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Targeting Alpha Synuclein Aggregates in Cutaneous Peripheral Nerve Fibers by Free-floating Immunofluorescence Assay
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Increased Aggregation Tendency of Alpha-Synuclein in a Fully Disordered Protein Complex.

David A Merle1, Anja Witternigg1, Carmen Tam-Amersdorfer2

  • 1Institute of Chemistry, University of Graz, Heinrichstr. 28, 8010 Graz, Austria.

Journal of Molecular Biology
|April 30, 2019
PubMed
Summary

Random fuzzy protein interactions, though flexible, can drive toxic aggregation. This study reveals how alpha-Synuclein and SERF1a complexes expose amyloid nucleation sites, increasing aggregation risk and disease association.

Keywords:
Alpha synucleinAmyloidsFuzzy complexesIntrinsically disordered proteinsMOAG-4/SERF

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Biologically active disordered protein complexes, termed random fuzzy interactions, present a paradox regarding their link to protein aggregation and misfolding.
  • The intrinsically disordered proteins alpha-Synuclein (aSyn) and SERF1a are implicated in neurodegenerative diseases, but the structural basis of their pro-amyloid activity remains unclear.

Purpose of the Study:

  • To elucidate the structural mechanism by which the aSyn:SERF1a random fuzzy complex potentiates cytotoxic aggregation.
  • To understand how the inherent flexibility of such complexes influences pathological misfolding and amyloid formation.

Main Methods:

  • Integrated Nuclear Magnetic Resonance (NMR) and Small-Angle X-ray Scattering (SAXS) analyses were employed to model the aSyn:SERF1a complex.
  • Structural characterization of the reconstituted complex to identify key interaction interfaces and conformational dynamics.

Main Results:

  • A structural model revealed partial deprotection of a specific alpha-Synuclein amyloid nucleation element within the disordered aSyn:SERF1a ensemble.
  • This minimal exposure of the nucleation site significantly increased the amyloidogenic tendency of SERF1a-bound alpha-Synuclein.
  • The findings explain the previously observed pro-amyloid activity of SERF1a.

Conclusions:

  • Random fuzziness in protein-protein interactions can initiate highly organized, disease-associated processes like amyloid polymerization.
  • This study provides a structural basis for how disordered protein complexes can trigger pathological misfolding and aggregation, relevant to neurodegenerative diseases.