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Investigation of protein-induced formation of lipid domains and their dynamics using fluorescence energy transfer

UNCW Author/Contributor (non-UNCW co-authors, if there are any, appear on document)
Jenny R. Wright (Creator)
Institution
The University of North Carolina Wilmington (UNCW )
Web Site: http://library.uncw.edu/
Advisor
Paulo Almeida

Abstract: An important feature in the current understanding of membrane structure is the existence of lipid domains. Lipid domain formation was observed in an experimental lipid bilayer system containing an equilibrium mixture of glycerophospholipids and raft lipids. Protein-lipid interactions in the equilibrium mixtures were observed when a peripheral membrane peptide was added. These interactions were measured using fluorescence energy transfer. Domain formation as a function of time was also investigated after the protein was added to the equilibrium mixture using stopped-flow fluorescence. Domain formation in vesicles containing 40% anionic lipid occurred in less than 1 s. Domain dissipation was observed with stopped flow fluorescence spectroscopy in glycerophospholipid vesicles as well as in a mixture of glycerophospholipids and raft lipids by removing the peptide. Domain dissipation in vesicles containing glycerophospholipids with 20% anionic lipid occurred in approximately 5 s. Domain dissipation in vesicles containing rafts and 40% anionic lipid occurred in approximately 900 s and domain dissipation in vesicles containing rafts and 10% anionic lipid occurred in approximately 160 s. These timescales were compared to the off-rate of the peptide from the vesicles.

Additional Information

Publication
Thesis
A Thesis Submitted to the University of North Carolina Wilmington in Partial Fulfillment Of the Requirements for the Degree of Master of Science
Language: English
Date: 2009
Keywords
Analytical biochemistry, Bilayer lipid membranes--Analysis, Fluorescence spectroscopy, Proteins--Analysis
Subjects
Fluorescence spectroscopy
Analytical biochemistry
Bilayer lipid membranes -- Analysis
Proteins -- Analysis