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

FEBS Letters

Fink, Anthony L.¹  Uversky, Vladimir N.¹  Li, Jie¹ 

[1] Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA

关键词: α-Synuclein;    Fibril;    Osmolyte;    Natively unfolded;    Trimethylamine-N-oxide;    Oligomer;   

DOI  :  10.1016/S0014-5793(01)03121-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effect of the natural osmolyte trimethylamine-N-oxide (TMAO) on the structural properties and fibril formation of the natively unfolded protein human α-synuclein was studied using several physico-chemical methods. TMAO induced folding of α-synuclein: at moderate concentrations, a partially folded intermediate with enhanced propensity for fibrillation accumulated; at higher concentrations, α-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.

【 授权许可】

Unknown