Fluorescence Studies of Exchangeable Apolipoprotein-Lipid Interactions

Protein-lipid interactions of apolipophorin-III, a model exchangeable amphipathic apolipoprotein.

A molecular trigger of lipid binding-induced opening of a helix bundle exchangeable apolipoprotein.

Apolipophorin III (apoLp-III) from the sphinx moth, Manduca sexta, is a helix bundle protein that interacts reversibly with lipoproteins. Its five elongated amphipathic alpha-helices are organized in an antiparallel fashion, with helices 3 and 4 connected by a short 6-residue (PDVEKE) linker helix, termed helix 3'. Upon interaction with lipoproteins, apoLp-III opens to expose a continuous hydro...

New BODIPY lipid probes for fluorescence studies of membranes.

Many fluorescent lipid probes tend to loop back to the membrane interface when attached to a lipid acyl chain rather than embedding deeply into the bilayer. To achieve maximum embedding of BODIPY (4,4-difluoro-4-bora-3a,4a-diaza-s-indacene) fluorophore into the bilayer apolar region, a series of sn-2 acyl-labeled phosphatidylcholines was synthesized bearing 4,4-difluoro-1,3,5,7-tetramethyl-4-bo...

Interactions in Lipid-water Interface Assessed by Fluorescence Spectroscopy

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Steady-state fluorescence studies on lipase-vesicle interactions.

The interaction of lipase from Candida cylindracea (CCL) with positively charged polymerizable surfactant vesicles was studied by the use of steady-state fluorescence techniques. The phase transition of vesicles composed of nonpolymerized and polymerized N-allylbis[2-(hexadecanoyloxy)ethyl]methylammonium bromide (ABHEMA Br) was determined in the absence of lipase, by measuring the change in flu...