Domain formation in choleterol/POPE/POPC lipid bilayer membranes

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dc.contributor.committeeChairVaughn, Mark W.
dc.contributor.committeeMemberDai, Lenore L.
dc.contributor.committeeMemberCheng, Kelvin K.
dc.creatorThiagarajan, Visveswaran
dc.date.accessioned2016-11-14T23:23:17Z
dc.date.available2011-02-18T21:38:42Z
dc.date.available2016-11-14T23:23:17Z
dc.date.issued2005-08
dc.degree.departmentChemical Engineeringen_US
dc.description.abstractThe regulation of several activities of the cell membranes has been associated with the formation of membrane domains. Self assembling lipid bilayers that serve as model cell membranes have been used to study their lateral organization and the formation of such lateral membrane domains. A recently proposed Superlattice (SL) model and several experimental studies have shown that Cholesterol and several lipids molecules tend to form an ordered domain at certain critical compositions as predicted by the SL model. Cholesterol/POPE/POPC lipid bilayers were used in this work and their lateral organization and the formation of membrane domains was studied using steady state and time-resolved fluorescence spectroscopy. The peaks and dips obtained in the values of the steady state anisotropy and the parameters obtained from the time-resolved studies serve as evidence indicating the formation of ordered domains at the head group and acyl chain level. An attempt was made to study the effect of the formation of such membrane domains on the binding of proteins to the membrane. A glass microfluidic chip was fabricated for this purpose. The binding of the proteins to the supported bilayers in the microchannels of the biochip was studied using total internal refraction fluorescence microscopy.
dc.format.mimetypeapplication/pdf
dc.identifier.urihttp://hdl.handle.net/2346/16627en_US
dc.language.isoeng
dc.publisherTexas Tech Universityen_US
dc.rights.availabilityUnrestricted.
dc.subjectSuperlattice modelen_US
dc.subjectMembrane domainsen_US
dc.subjectLipid bilayersen_US
dc.titleDomain formation in choleterol/POPE/POPC lipid bilayer membranes
dc.typeThesis

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