Temperature dependence of the size of phospholipid vesicles

Cornell, Bruce; Fletcher, Guy C.; Middlehurst, J.; Separovic, Frances

doi:10.1016/0005-2736(81)90453-3

Cited by 23 publications

(6 citation statements)

References 13 publications

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“…It should be noted that the radius of the 1 mol % cholesterol-DMPC vesicles is similar at 4 and 37 °C by negative-stain electron microscopy (cf. Watts et al, 1978;Cornell et al, 1981). The size distribution of 1 mol % cholesterol-DMPC bilayer vesicles on Sepharose CL-2B columns is also similar to that of egg yolk PC vesicles at 37 °C, but a small amount of fusion is evident on the columns when run at 4 °C.…”

Section: Resultsmentioning

confidence: 88%

Cholesterol desorption from clusters of phosphatidylcholine and cholesterol in unilamellar vesicle bilayers during lipid transfer or exchange

McLean¹,

Phillips²

1982

Biochemistry

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Section: Resultsmentioning

confidence: 88%

Cholesterol desorption from clusters of phosphatidylcholine and cholesterol in unilamellar vesicle bilayers during lipid transfer or exchange

McLean¹,

Phillips²

1982

Biochemistry

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“…In a previous study of nystatin interaction with gel phase The calculation of the average number of lipids in a single liposome, m, was based upon a 4.5-nm bilayer thickness, an average surface area occupied by each phospholipid molecule of 0.7 nm 2 (fluid phase) (Marsh, 1990;Nagle and Wiener, 1988) and assuming an homogeneous population of spherical lipid vesicles. It was also considered that there were no phospholipid packing constraints in the smaller vesicles and that the temperature did not influence the average number of lipids per liposome (Cornell et al, 1981).…”

Section: Nystatin Interaction With Dppc and Popc Luvmentioning

confidence: 99%

Cooperative Partition Model of Nystatin Interaction with Phospholipid Vesicles

Coutinho

Prieto²

2003

Biophysical Journal

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Nystatin is a membrane-active polyene antibiotic that is thought to kill fungal cells by forming ion-permeable channels. In this report we have investigated nystatin interaction with phosphatidylcholine liposomes of different sizes (large and small unilamellar vesicles) by time-resolved fluorescence measurements. Our data show that the fluorescence emission decay kinetics of the antibiotic interacting with gel-phase 1,2-dipalmitoyl-sn-glycero-3-phosphocholine vesicles is controlled by the mean number of membrane-bound antibiotic molecules per liposome, . The transition from a monomeric to an oligomeric state of the antibiotic, which is associated with a sharp increase in nystatin mean fluorescence lifetime from approximately 7-10 to 35 ns, begins to occur at a critical concentration of 10 nystatin molecules per lipid vesicle. To gain further information about the transverse location (degree of penetration) of the membrane-bound antibiotic molecules, the spin-labeled fatty acids (5- and 16-doxyl stearic acids) were used in depth-dependent fluorescence quenching experiments. The results obtained show that monomeric nystatin is anchored at the phospholipid/water interface and suggest that nystatin oligomerization is accompanied by its insertion into the membrane. Globally, the experimental data was quantitatively described by a cooperative partition model which assumes that monomeric nystatin molecules partition into the lipid bilayer surface and reversibly assemble into aggregates of 6 +/- 2 antibiotic molecules.

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“…Some of its properties include being antimicrobial 43 [5], cytolytic [6,7], cationic (+5) and hemolytic [8,9]. The MLT peptide 44 has an amphipathic structure [10,11], a strong binding affinity to lipid 45 membranes [12] and can exist in two orientations, parallel or perpen- 46 dicular to the membrane bilayer [13]. Furthermore, MLT is known to 47 induce changes in the integrity of plasma membranes and lipid bilayers 48 resulting in pore and ion channel formation as well as vesicle deforma- 49 tion [4,14].…”

mentioning

confidence: 99%

Site of fluorescent label modifies interaction of melittin with live cells and model membranes

Jamasbi

Ciccotosto

Tailhades

et al. 2015

Biochimica et Biophysica Acta (BBA) - Biomembranes

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The mechanism of membrane disruption by melittin (MLT) of giant unilamellar vesicles (GUVs) and live cells was studied using fluorescence microscopy and two fluorescent synthetic analogues of MLT. The N-terminus of one of these was acylated with thiopropionic acid to enable labeling with maleimido-AlexaFluor 430 to study the interaction of MLT with live cells. It was compared with a second analogue labeled at P14C. The results indicated that the fluorescent peptides adhered to the membrane bilayer of phosphatidylcholine GUVs and inserted into the plasma membrane of HeLa cells. Fluorescence and light microscopy revealed changes in cell morphology after exposure to MLT peptides and showed bleb formation in the plasma membrane of HeLa cells. However, the membrane disruptive effect was dependent upon the location of the fluorescent label on the peptide and was greater when MLT was labeled at the N-terminus. Proline at position 14 appeared to be important for antimicrobial activity, hemolysis and cytotoxicity, but not essential for cell membrane disruption.

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Temperature dependence of the size of phospholipid vesicles

Cited by 23 publications

References 13 publications

Cholesterol desorption from clusters of phosphatidylcholine and cholesterol in unilamellar vesicle bilayers during lipid transfer or exchange

Cholesterol desorption from clusters of phosphatidylcholine and cholesterol in unilamellar vesicle bilayers during lipid transfer or exchange

Cooperative Partition Model of Nystatin Interaction with Phospholipid Vesicles

Site of fluorescent label modifies interaction of melittin with live cells and model membranes

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