1 January 1987 Pyrene-Labeled Amphiphiles: Dynamic And Structural Probes Of Membranes And Lipoproteins
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Proceedings Volume 0743, Fluorescence Detection; (1987) https://doi.org/10.1117/12.966938
Event: OE LASE'87 and EO Imaging Symposium, 1987, Los Angeles, CA, United States
Lipids and proteins are important functional and structural components of living organisms. Although proteins are frequently found as soluble components of plasma or the cell cytoplasm, many lipids are much less soluble and separate into complex assemblies that usually contain proteins. Cell membranes and plasma lipoproteins' are two important macro-molecular assemblies that contain both lipids and proteins. Cell membranes are composed of a variety of lipids and proteins that form an insoluble bilayer array that has relatively little curvature over distances of several nm. Plasma lipoproteins are different in that they are much smaller, water-soluble, and have highly curved surfaces. A model of a high density lipoprotein (HDL) is shown in Figure 1. This model (d - 10 nm) contains a surface of polar lipids and proteins that surrounds a small core of insoluble lipids, mostly triglycerides and cholesteryl esters. The low density (LDL) (d - 25 nm) and very low density (VLDL) (d 90 nm) lipoproteins have similar architectures, except the former has a cholesteryl ester core and the latter a core that is almost exclusively triglyceride (Figure 1). The surface proteins of HDL are amphiphilic and water soluble; the single protein of LDL is insoluble, whereas VLDL contains both soluble and insoluble proteins. The primary structures of all of these proteins are known.
© (1987) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Henry J. Pownall, Henry J. Pownall, Reynold Homan, Reynold Homan, John B. Massey, John B. Massey, } "Pyrene-Labeled Amphiphiles: Dynamic And Structural Probes Of Membranes And Lipoproteins", Proc. SPIE 0743, Fluorescence Detection, (1 January 1987); doi: 10.1117/12.966938; https://doi.org/10.1117/12.966938

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