We have located links that may give you full text access.
Electrochemical detection of interaction between copper(II) and peptides related to pathological α-synuclein mutants.
Analytical Chemistry 2019 Februrary 20
Herein we present a proof of concept study for electrochemical detection of the metal-binding site of α-synuclein (α-syn). Parkinson's disease (PD) is associated with the aggregation and misfolding of α-syn in dopaminergic neurons. Since copper homeostasis is deregulated in PD, it is of great significance to study the metal-binding site of wild-type (WT) α-syn (48-53, VVHGVA), and its pathological mutants (H50Q, and G51D). Cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS) were used to monitor the formation of peptide-PEG mixed layer on gold surfaces. Differential pulse voltammetry (DPV) was used to detect and evaluate the interaction of copper(II) with the peptide layer. X-ray photoelectron spectroscopy (XPS) was used to characterize the formation and attachment of the peptide layer on gold surfaces. Isothermal titration calorimetry (ITC) was also utilized to evaluate the binding characteristics of the peptides with copper(II) ions. Our results indicated that the effect of a single amino acid mutation on the peptides drastically influenced their ability to interact with copper(II) ions. These results demonstrated that our electrochemical approach provided a rapid and cost-effective platform to study the strong interaction between α-syn and copper(II), which is implicated as one of the factors inducing structural changes in α-syn towards the progression of PD.
Full text links
Related Resources
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