TITLE:
Fluorescence as a Tool to Study Lipid-Protein Interactions: The Case of α-Synuclein
AUTHORS:
Azucena Gonzalez-Horta, Brenda Gonzalez Hernandez, Abelardo Chavez-Montes
KEYWORDS:
Fluorescence Spectroscopy; Lipid-Protein Interactions; α-Synuclein
JOURNAL NAME:
Open Journal of Biophysics,
Vol.3 No.1A,
February
27,
2013
ABSTRACT:
During the past 20 years there has been a remarkable growth in the use
of fluorescence in the biological sciences. Fluorescence is now a dominant
methodology used extensively in biochemistry, biophysics, biotechnology, medical
diagnostics, flow cytometry, DNA sequencing and genetic analysis to name
a few. It is one of the most powerful methods to study protein folding, dynamics,
assembly and interactions as well as membrane structure. α-Synuclein belongs to the class of intrinsically disordered proteins
lacking of a well-folded structure under physiological conditions. The conversion of α-synuclein from a soluble monomer to
an insoluble fibril may underlie the neurodegeneration associated with Parkinson’s
disease (PD). Although the exact mechanism of α-synuclein toxicity is still unknown, it has been proposed that disturbs
membrane structure, leading to increased membrane permeability and eventual cell
death. This review highlights the significant role played by fluorescence techniques
in unraveling the nature of interactions between α-synuclein and membranes and its implications in PD.