Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  DetailsÜbersicht

Freigegeben
Zeitschriftenartikel

Small molecule-induced soluble oligomers of α-synuclein with helical structure.

MPG-Autoren
/persons/resource/persons79054

Fonseca-Ornelas,  L.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons198417

Schmidt,  C. D.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons104964

Camacho-Zarco,  A. R.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons15063

Fernandez,  C. O.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons14824

Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons16093

Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

Externe Ressourcen
Es sind keine externen Ressourcen hinterlegt
Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)

2468397_Suppl.pdf
(Ergänzendes Material), 4MB

Zitation

Fonseca-Ornelas, L., Schmidt, C. D., Camacho-Zarco, A. R., Fernandez, C. O., Becker, S., & Zweckstetter, M. (2017). Small molecule-induced soluble oligomers of α-synuclein with helical structure. Chemistry-A European Journal, (53), 13010-13014. doi:10.1002/chem.201703001.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002D-B1DE-3
Zusammenfassung
Accumulation of α-synuclein (αSyn) aggregates constitutes the hallmark of synucleinopathies including Parkinson's disease. However, many steps from the innocuous, monomeric αSyn toward misfolded oligomers and fibrillar species remain unclear. Here, we show that αSyn can form in solution α-helical oligomers, which are off-pathway to fibrillization, through interaction with the tetrapyrrole phthalocyanine tetrasulfonate. Chemical cross-linking combined with mass spectrometry reveals a large number of intermolecular cross-links along the entire αSyn sequence in the phthalocyanine tetrasulfonate-stabilized αSyn oligomers. Our study suggests that stabilization of structured oligomers by small molecules provides a viable strategy to interfere with αSyn fibrillization.