Abstract
Parkinson's Disease is characterized by the presence of fibrillar deposits of alpha-Synuclein (αS) in the substantia nigra. αS is an intrinsically unstructured protein that becomes α-helical upon binding lipid membranes. Many studies indicate that the toxic form of αS may be pre-fibrillar oligomers formed in solution or upon binding to cell membranes or synaptic vesicles. The effects of curvature and lipid composition on αS binding were studied by using Fluorescence Correlation Spectroscopy (FCS) to quantitatively measure the binding affinity of αS for synthetic lipid vesicles.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
