Trimethylamine-n-oxide-induced Folding of α-synuclein

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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.

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FEBS Letters, v. 509, issue 1, p. 31-35