Cited by 208Parkinson's Disease Mechanisms and TreatmentsProtein Structure and DynamicsProtein purification and stability

Trimethylamine‐ N ‐oxide‐induced folding of α‐synuclein

Uversky, Vladimir N., Li, Jie, Fink, Anthony L.·2001·FEBS Letters

Abstract

The effect of the natural osmolyte trimethylamine-N-oxide (TMAO) on the structural properties and fibril formation of the natively unfolded protein human alpha-synuclein was studied using several physico-chemical methods. TMAO induced folding of alpha-synuclein: at moderate concentrations, a partially folded intermediate with enhanced propensity for fibrillation accumulated; at higher concentrations, alpha-synuclein was tightly folded and underwent self-association to form oligomers. The latter conformation was significantly helical and probably represents the physiologically folded form of the protein.

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Crossref · 10.1016/s0014-5793(01)03121-0

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33 of 33 references verified0 citation errors · 0 not checkable

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Authors
Uversky, V. N., Li, J., & Fink, A. L.
Affiliations
  • Russian Academy of Sciences (RU)
  • University of California, Santa Cruz (US)
Corresponding author
Fink, Anthony L.
Venue
FEBS Letters
Publisher
Wiley
Published
2001-11-09
Volume
509
Issue
1
Pages
31-35
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W1988949963
Cited by
208
References
34
Citations by year
2026: 9 · 2025: 13 · 2024: 11 · 2023: 5 · 2022: 12 · 2021: 8 · 2020: 10 · 2019: 7 · 2018: 8 · 2017: 8 · 2016: 8 · 2015: 8 · 2014: 12 · 2013: 10 · 2012: 11
FWCI
3.54
Type
journal article
Language
en
Open access
closed
Locations
  • FEBS Letters (publishedVersion)
  • PubMed (publishedVersion)
  • Digital Commons - University of South Florida (University of South Florida) (submittedVersion)
Topics
  • Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
Keywords
trimethylamine N-oxide, alpha-synuclein, protein folding, osmolytes, intrinsically disordered proteins, fibril formation, folding intermediates, oligomerization, helical conformation, protein self-association
MeSH terms
Acrylamides, Circular Dichroism, Dose-Response Relationship, Drug, Methylamines, Nerve Tissue Proteins, Peptides, Protein Conformation, Recombinant Proteins, Scattering, Radiation, Spectrometry, Fluorescence, Time Factors, X-Rays, Oxidants, Protein Structure, Secondary, Protein Folding, Synucleins, alpha-Synuclein

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