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• W2059053571 endingPage "8507" @default.
• W2059053571 startingPage "8497" @default.
• W2059053571 abstract "We report a study of the interactions of proteins with monolayers of phospholipids (D/L-alpha-dipalmitoyl phosphatidylcholine and L-alpha-dilauroyl phosphatidylcholine) spontaneously assembled at an interface between an aqueous phase and a 20-microm-thick film of a nematic liquid crystal (4'-pentyl-4-cyanobiphenyl). Because the orientation of the liquid crystal is coupled to the organization of the lipids, specific interactions between phospholipase A2 and the lipids (binding and/or hydrolysis) that lead to reorganization of the lipids are optically reported (using polarized light) as dynamic orientational transitions in the liquid crystal. In contrast, nonspecific interactions between proteins such as albumin, lysozyme, and cytochrome-c and the lipid-laden interface of the liquid crystal are not reported as orientational transitions in the liquid crystals. Concurrent epifluorescence and polarized light imaging of labeled lipids and proteins at the aqueous-liquid crystal interface demonstrate that spatially patterned orientations of the liquid crystals observed during specific binding of phospholipase A2 to the interface, as well as during the subsequent hydrolysis of lipids by phospholipase A2, reflect the lateral organization (micrometer-sized domains) of the proteins and lipids, respectively, at the aqueous-liquid crystal interface." @default.
• W2059053571 created "2016-06-24" @default.
• W2059053571 creator A5014198121 @default.
• W2059053571 creator A5024432725 @default.
• W2059053571 date "2007-06-27" @default.
• W2059053571 modified "2023-09-30" @default.
• W2059053571 title "Coupling of the Orientations of Thermotropic Liquid Crystals to Protein Binding Events at Lipid-Decorated Interfaces" @default.
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• W2059053571 doi "https://doi.org/10.1021/la0634286" @default.
• W2059053571 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17595119" @default.
• W2059053571 hasPublicationYear "2007" @default.
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