We have located links that may give you full text access.
Coordination of platinum to α-synuclein inhibits filamentous aggregation in solution.
Chembiochem : a European Journal of Chemical Biology 2019 April 9
Accumulation of filamentous aggregates of α-synuclein (AS) in Lewy bodies and neurites characterizes neurodegenerative diseases such as Parkinson's disease. Inhibition of AS fibrillation is helpful for understanding of AS aggregate structure and for developing chemical therapies. Herein we report that the Pt(II)-containing antitumor drug cisplatin suppresses filamentous aggregation of AS in solution. Pt(II) contrasts strongly with reported transition-metal ions such as Mn(II), Fe(III), and Cu(II), which accelerate AS aggregation. Interaction of Pt(II) with sidechains of methionine and histidine residues was essential for inhibition of AS fibrillation. Binding of Pt(II) to AS did not change the polypeptide's overall random coil structure, as indicated by solution-state two-dimensional NMR and circular dichroism spectroscopy; and a solution of the AS-Pt(II) complex remained free of filamentous aggregates. Our results constitute interesting new information about the biological chemistry of metal ions in Parkinson's disease and may open new lines of research on the suppression of the filamentous aggregation.
Full text links
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.
By using this service, you agree to our terms of use and privacy policy.
Your Privacy Choices
You can now claim free CME credits for this literature searchClaim now
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app