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Influence of protein and lipid domains on the structure, fluidity and phase behavior of lipid bilayer membranes

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dc.contributor.advisor Alice P. Gast. en_US
dc.contributor.author Horton, Margaret R. (Margaret Ruth) en_US
dc.contributor.other Massachusetts Institute of Technology. Dept. of Chemical Engineering. en_US
dc.date.accessioned 2007-09-28T13:25:59Z
dc.date.available 2007-09-28T13:25:59Z
dc.date.copyright 2006 en_US
dc.date.issued 2007 en_US
dc.identifier.uri http://hdl.handle.net/1721.1/38982
dc.description Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemical Engineering, February 2007. en_US
dc.description Includes bibliographical references (p. 136-148). en_US
dc.description.abstract The lipid bilayer forms the basic structure of the cell membrane, which is a heterogeneous matrix of proteins and lipids that provides a barrier between the interior of a cell and its outside environment. Protein and lipid domains in cell membranes can facilitate receptor localization, stabilize membranes, and influence membrane fluidity. In this thesis, we study how ordered protein and lipid domains influence the physical properties of lipid bilayers to better understand the roles of membrane domains in biological mechanisms. Model cellular membranes that mimic the behavior of biological membranes offer a controllable environment for systematically studying the isolated effects of protein and lipid ordering on membrane organization. Using fluid and solid-supported lipid bilayers, we study ordered peripheral membrane proteins and lateral lipid phase separation with fluorescence microscopy and X-ray reflectivity. To model cellular protein coatings and peripheral proteins, we prepare biotin-functionalized membranes that bind the proteins streptavidin and avidin. Fluorescence microscopy studies demonstrate that proteins crystallized in a single layer on lipid bilayer surfaces can change the lipid curvature and stabilize lipid vesicles against osmotic collapse. en_US
dc.description.abstract (cont.) At solid interfaces, we characterize the electron density profiles of protein-coated bilayers to determine how a water layer separates an immobile protein layer from the fluid lipid bilayer. Liquid-ordered lipid phases enriched in cholesterol and sphingomyelin can localize molecules in cell membranes and this lipid phase separation behavior may be influenced by proteins and molecules in the membrane. Caveolae are specialized liquid-ordered domains in the plasma membrane that are enriched in the protein caveolin-1. We demonstrate that caveolin-1 peptides influence the onset of lipid phase separation and bind phase-separated lipid bilayers in solution. On solid surfaces, the formation of liquid-ordered lipid phases is influenced by surface roughness; with reflectivity, we determine that lipid bilayers containing cholesterol and sphingomyelin thicken with increasing cholesterol content. The membrane receptor GM1 also thickens the lipid bilayer when it is incorporated into the bilayer upper leaflet. The diverse experimental platforms that we present are applicable to studying additional and more complex biological systems to elucidate the influence of lipid and protein domains on cell membrane structure, organization and fluidity. en_US
dc.description.statementofresponsibility by Margaret R. Horton. en_US
dc.format.extent 148 p. en_US
dc.language.iso eng en_US
dc.publisher Massachusetts Institute of Technology en_US
dc.rights M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission. en_US
dc.rights.uri http://dspace.mit.edu/handle/1721.1/7582
dc.subject Chemical Engineering. en_US
dc.title Influence of protein and lipid domains on the structure, fluidity and phase behavior of lipid bilayer membranes en_US
dc.type Thesis en_US
dc.description.degree Ph.D. en_US
dc.contributor.department Massachusetts Institute of Technology. Dept. of Chemical Engineering. en_US
dc.identifier.oclc 166351561 en_US


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