Issue 4, 2021
From the journal:

RSC Chemical Biology

Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy†

Sanjib K. Mukherjee,‡a   Jim-Marcel Knop,‡a   Rosario Oliva,a   Simone Möbitza  and  Roland Winter ORCID logo *a  

* Corresponding authors

a Physical Chemistry I-Biophysical Chemistry, Department of Chemistry and Chemical Biology, TU Dortmund University, Otto-Hahn Strasse 4a, Dortmund D-44227, Germany
E-mail: roland.winter@tu-dortmund.de

Abstract

The intrinsically disordered protein α-synuclein causes Parkinson's disease by forming toxic oligomeric aggregates inside neurons. Single-molecule FRET experiments revealed conformational changes of noncanonical DNA structures, such as i-motifs and hairpins, in the presence of α-synuclein. Volumetric analyses revealed differences in binding mode, which is also affected by cellular osmolytes.

Graphical abstract: Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy

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Article information

DOI
https://doi.org/10.1039/D1CB00108F
Article type
Communication
Submitted
14 May 2021
Accepted
01 Jul 2021
First published
02 Jul 2021
This article is Open Access
Creative Commons BY license

RSC Chem. Biol., 2021,2, 1196-1200

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Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy

S. K. Mukherjee, J. Knop, R. Oliva, S. Möbitz and R. Winter, RSC Chem. Biol., 2021, 2, 1196 DOI: 10.1039/D1CB00108F

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