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

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. Volu...

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Detalles Bibliográficos
Autores principales: Mukherjee, Sanjib K., Knop, Jim-Marcel, Oliva, Rosario, Möbitz, Simone, Winter, Roland
Formato: Online Artículo Texto
Lenguaje:English
Publicado: RSC 2021
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8341996/
https://www.ncbi.nlm.nih.gov/pubmed/34458831
http://dx.doi.org/10.1039/d1cb00108f
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author Mukherjee, Sanjib K.
Knop, Jim-Marcel
Oliva, Rosario
Möbitz, Simone
Winter, Roland
author_facet Mukherjee, Sanjib K.
Knop, Jim-Marcel
Oliva, Rosario
Möbitz, Simone
Winter, Roland
author_sort Mukherjee, Sanjib K.
collection PubMed
description 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.
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spelling pubmed-83419962021-08-26 Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy Mukherjee, Sanjib K. Knop, Jim-Marcel Oliva, Rosario Möbitz, Simone Winter, Roland RSC Chem Biol Chemistry 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. RSC 2021-07-02 /pmc/articles/PMC8341996/ /pubmed/34458831 http://dx.doi.org/10.1039/d1cb00108f Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/
spellingShingle Chemistry
Mukherjee, Sanjib K.
Knop, Jim-Marcel
Oliva, Rosario
Möbitz, Simone
Winter, Roland
Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy
title Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy
title_full Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy
title_fullStr Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy
title_full_unstemmed Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy
title_short Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy
title_sort untangling the interaction of α-synuclein with dna i-motifs and hairpins by volume-sensitive single-molecule fret spectroscopy
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8341996/
https://www.ncbi.nlm.nih.gov/pubmed/34458831
http://dx.doi.org/10.1039/d1cb00108f
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