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1.
Biophys Chem ; 92(3): 155-68, 2001 Sep 18.
Article in English | MEDLINE | ID: mdl-11583833

ABSTRACT

Resonance energy transfer involving tryptophan as a donor and anthrylvinyl-labeled phosphatidylcholine (AV-PC), 3-methoxybenzanthrone (MBA) and 8-anilino-1-naphthalene sulfonic acid (ANS) as acceptors has been examined to obtain information on the structure of peptide-lipid systems consisting of 18A or Ac-18A-NH(2) peptides and large unilamellar phosphatidylcholine vesicles. The lower and upper limits for the tryptophan distance from the bilayer midplane have been assessed in terms of the models of energy transfer in two-dimensional systems, taking into account orientational effects. Evidence for the existence of preferential orientations of Ac-18A-NH(2) with respect to the lipid-water interface has been obtained.


Subject(s)
Lipids/chemistry , Peptides/chemistry , Algorithms , Anisotropy , Energy Transfer , Fluorescence , Lipid Bilayers , Models, Theoretical , Tryptophan/chemistry
2.
Biofizika ; 45(1): 58-64, 2000.
Article in Russian | MEDLINE | ID: mdl-10732211

ABSTRACT

Complexes of ribonuclease, lysozyme, cytochrome c and hemoglobin with model phospholipid membranes composed of phosphatidylcholine and diphosphatidylglycerol (4:3, mol:mol) were investigated by the method of non-radiative fluorescence energy transfer. Evidence for the penetration of proteins in to the lipid bilayer interior was obtained. The size of the protein fragment incorporated into the polar membrane region was estimated.


Subject(s)
Energy Transfer , Lipid Bilayers/chemistry , Phospholipids/chemistry , Proteins/chemistry , Cardiolipins/chemistry , Cytochrome c Group/chemistry , Fluorescent Dyes , Hemoglobins/chemistry , Muramidase/chemistry , Phosphatidylcholines/chemistry , Ribonucleases/chemistry
3.
Biophys Chem ; 81(2): 93-105, 1999 Oct 04.
Article in English | MEDLINE | ID: mdl-10515045

ABSTRACT

By examining the resonance energy transfer between fluorescent probes, embedded in the lipid bilayer (4-(dimethylaminostyryl)-1-methylpiridine, 4-(dimethylaminostyryl)-1-dodecylpiridine, N,N'-bishexamethylenrhodamine, rhodamine 6G) as donors, and the heme group of hemoglobin as acceptor, the structure of the protein complexes with the model membranes composed of phosphatidylcholine and cardiolipin was characterized. Quantitative interpretation of the experimental data was performed in terms of the model of energy transfer in two-dimensional systems, using a set of parameters including the distance of closest approach between donor and acceptor, the vertical separation of donor planes, the acceptor distance from the donor plane and the orientation factor. The limits for the heme distance from the lipid bilayer center and the depth of the protein penetration in the membrane interior were estimated. The results obtained suggest that the depth of hemoglobin insertion into liposomal membranes decreases upon increasing CL content in the lipid bilayer.


Subject(s)
Hemoglobins/chemistry , Lipid Bilayers/chemistry , Phospholipids/chemistry , Animals , Benzenesulfonates/chemistry , Cardiolipins/chemistry , Cattle , Fluorescent Dyes/chemistry , Heme/chemistry , Liposomes , Models, Biological , Models, Chemical , Phosphatidylcholines/chemistry , Pyridinium Compounds/chemistry
4.
Biochim Biophys Acta ; 1420(1-2): 1-13, 1999 Aug 20.
Article in English | MEDLINE | ID: mdl-10446285

ABSTRACT

Resonance energy transfer between a series of lipid-bound fluorescent probes as donors and the heme group of cytochrome c as acceptor has been used to obtain structural information on the protein complexes with model membranes, composed of phosphatidylcholine and cardiolipin. Analysis of experimental data in terms of the model of energy transfer in two-dimensional systems provides further evidence for preferential cytochrome c orientation with respect to the lipid bilayer and penetration of the protein into the membrane interior.


Subject(s)
Cytochrome c Group/chemistry , Phospholipids/chemistry , Animals , Cardiolipins/chemistry , Cattle , Energy Transfer , In Vitro Techniques , Lipid Bilayers/chemistry , Liposomes/chemistry , Macromolecular Substances , Models, Chemical , Phosphatidylcholines/chemistry
5.
Biofizika ; 44(2): 257-62, 1999.
Article in Russian | MEDLINE | ID: mdl-10418676

ABSTRACT

The method of radiationless energy transfer was used to study the structure of lysozyme complexes with liposomes composed of phosphatidylcholine and diphosphatidylglycerol (4:3, mol:mol). 4-(n-Dimethylaminostyryl)-1-methylpyridinium n-toluenesulfonate, 4-(n-dimethylaminostyryl)-1-hexylpyridinium n-toluenesulfonate, 4-(n-dimethylaminostyryl)-1-dodecylpyridinium n-toluenesulfonate, and 3-metoxybenzanthrone were used as donors, and nile blue and rhodamine 6G, as acceptors. An increase in the surface area of model membranes upon binging of the protein to lipid bilayer was found.


Subject(s)
Liposomes/chemistry , Muramidase/chemistry , Energy Transfer , Fluorescent Dyes , Phospholipids/chemistry
6.
Biofizika ; 44(6): 1048-53, 1999.
Article in Russian | MEDLINE | ID: mdl-10707279

ABSTRACT

Using fluorescent probes DSM and DSP-12, the effect of ribonuclease and lysozyme on the structural state of liposomes composed of phosphatidylcholine and diphosphatidylglycerol was studied. A correlation between the changes in probe quantum yield and the amount of protein-bound lipids was established. It is assumed that the formation of protein-lipid complexes increases the packing density of lipids and restricts their mobility. As the content of diphosphatidylglycerol in the lipid bilayer increases, the condensing effect of proteins becomes more pronounced.


Subject(s)
Cardiolipins/chemistry , Liposomes/chemistry , Muramidase/chemistry , Phosphatidylcholines/chemistry , Ribonucleases/chemistry , Fluorescent Dyes
7.
Ukr Biokhim Zh (1978) ; 70(3): 68-72, 1998.
Article in Russian | MEDLINE | ID: mdl-9848183

ABSTRACT

Kinetics of methemoglobin structural changes in the complex with liposomes composed of phosphatidylcholine and its mixtures with cardiolipin has been studied. The amplitudes and rate constants of the two observed kinetic phases are determined. The fast kinetic phase is attributed to the formation of the unstable intermediate protein form, while the slow one is assumed to reflect dissociation of the heme--globin complex.


Subject(s)
Methemoglobin/chemistry , Kinetics , Liposomes , Protein Conformation
8.
Ukr Biokhim Zh (1978) ; 70(3): 109-13, 1998.
Article in Russian | MEDLINE | ID: mdl-9848191

ABSTRACT

Using tryptophan fluorescence quenching by iodide and acrylamide the effect of electrons with the energy 5 Mev on the structure of microsomal membrane proteins has been studied. Conformation of microsomal proteins were found to change upon irradiation.


Subject(s)
Electrons , Membrane Proteins/metabolism , Microsomes, Liver/radiation effects , Acrylamide/chemistry , Animals , Fluorescence , Iodides/chemistry , Membrane Proteins/chemistry , Protein Conformation , Rabbits , Tryptophan/chemistry
9.
Biochim Biophys Acta ; 1409(1): 12-24, 1998 Nov 02.
Article in English | MEDLINE | ID: mdl-9804870

ABSTRACT

The complexes of hemoglobin and cytochrome c with liposomes composed of phosphatidylcholine and its mixtures with cardiolipin and cholesterol have been studied by monitoring resonance energy transfer between fluorescent probe 3-methoxybenzanthrone as donor and heme groups of the proteins as acceptors. By analyzing experimental data within the framework of the model of energy transfer in two-dimensional systems, the limits of the range of possible heme positions with respect to lipid bilayer have been assessed. The distance of heme group of hemoglobin from the membrane center was found to increase in the presence of cardiolipin or cholesterol. The results obtained for cytochrome c complexes with cardiolipin-containing model membranes suggest the existence of preferential protein orientation relative to the lipid bilayer, and provide evidence for the protein penetration in the membrane interior.


Subject(s)
Cytochrome c Group/chemistry , Hemoglobins/chemistry , Lipids/chemistry , Benz(a)Anthracenes/metabolism , Cardiolipins/chemistry , Cholesterol/chemistry , Fluorescent Dyes/metabolism , Heme/chemistry , Lipid Bilayers/chemistry , Liposomes/chemistry , Phosphatidylcholines/chemistry , Spectrometry, Fluorescence
10.
Biochim Biophys Acta ; 1370(1): 107-18, 1998 Mar 06.
Article in English | MEDLINE | ID: mdl-9518571

ABSTRACT

The effect of methemoglobin on the structure of model membranes composed of phosphatidylcholine and diphosphatidylglycerol (18 : 1, mol : mol) was studied with the help of pH-indicator dye bromothymol blue. The partition coefficients characterizing the dye binding to methemoglobin or model membranes were derived from the pKaalpha dependences on the protein or phospholipid concentration. The observed character of the dye partitioning in the lipid or lipid-protein systems is interpreted in terms of the traditional electrostatic approach and some modern theories of membrane electrostatics. It is assumed that methemoglobin affects the structural and physicochemical parameters of lipid-water interface.


Subject(s)
Bromthymol Blue/chemistry , Hemoglobins/chemistry , Membranes, Artificial , Models, Chemical , Molecular Probes/chemistry , Animals , Horses , Hydrogen-Ion Concentration , Kinetics , Lipid Bilayers/chemistry , Membrane Proteins/chemistry , Methemoglobin/chemistry
11.
Biofizika ; 43(2): 260-3, 1998.
Article in Russian | MEDLINE | ID: mdl-9591100

ABSTRACT

The effect of ribonuclease and cytochrome c on electrophoretic mobility of liposomes composed of phosphatidylcholine and diphosphatidylglycerol has been studied. zeta-Potential of lipid vesicles was found to decrease in the presence of proteins. Parameters of proteins binding to phospholipids were evaluated from the changes of surface charge density of model membranes. The constants of protein association with phospholipids were calculated to be about 4 x 10(4) M-1 for ribonuclease and about 5.4 x 10(4) M-1 for cytochrome c.


Subject(s)
Cytochrome c Group/chemistry , Liposomes/chemistry , Ribonucleases/chemistry , Animals , Cattle , Electrophoresis, Polyacrylamide Gel
12.
Biofizika ; 42(4): 909-13, 1997.
Article in Russian | MEDLINE | ID: mdl-9410018

ABSTRACT

The effect of ribonuclease and lysozyme on pyrene excimerization in liposomes composed of phosphatidylcholine and diphosphatidylglycerol has been studied. Microviscosity of bulk and annular lipids was found to increase upon the formation of lipid-protein complexes.


Subject(s)
Lipid Bilayers/chemistry , Muramidase/chemistry , Ribonucleases/chemistry , Animals , Cattle , Liposomes , Viscosity
13.
Biofizika ; 41(5): 1038-43, 1996.
Article in Russian | MEDLINE | ID: mdl-9011184

ABSTRACT

Using fluorescent probe 4-(dimethylaminostyryl)-1-methylpridine n-toluenesulfonate (DSM) the effect of ribonuslease and lysozyme on the structure of liposomes composed of phosphatidylcholine and diphosphatidylglycerol has been studied. An analysis of DSM spectra contour has been carried out and parameters of inhomogeneous broadening has been estimated. Polarity of the probe surroundings was found to decrease upon lipid-protein complexes formation.


Subject(s)
Liposomes/chemistry , Muramidase/chemistry , Ribonucleases/chemistry , Fluorescent Dyes , Liposomes/metabolism , Muramidase/metabolism , Ribonucleases/metabolism
14.
Ukr Biokhim Zh (1978) ; 68(4): 105-8, 1996.
Article in Russian | MEDLINE | ID: mdl-9297296

ABSTRACT

The effect of triton X-100 and glutaraldehyde on the functioning of microsomal oxidoreductases has been investigated. Triton X-100 was found to increase the enzymes activity. The decrease of oxidoreductases activity was observed in the presence of glutaraldehyde.


Subject(s)
Glutaral/pharmacology , Intracellular Membranes/drug effects , Microsomes, Liver/drug effects , Octoxynol/pharmacology , Oxidoreductases/drug effects , Animals , Detergents , Microsomes, Liver/enzymology , Microsomes, Liver/ultrastructure , Rabbits
15.
Ukr Biokhim Zh (1978) ; 68(3): 111-6, 1996.
Article in Russian | MEDLINE | ID: mdl-9273720

ABSTRACT

Using fluorescent probes DSM, DSP-6 and DSP-12 interaction of methemoglobin with liposomes composed of phosphatidylcholine and diphosphatidylglycerol has been investigated. It was supposed that the observed decrease of probes fluorescence intensity is determined to some extent by lipids peroxidation.


Subject(s)
Fluorescent Dyes/chemistry , Liposomes/chemistry , Methemoglobin/chemistry , Pyridinium Compounds/chemistry , Lipid Peroxidation , Membranes, Artificial
16.
Biofizika ; 41(2): 355-62, 1996.
Article in Russian | MEDLINE | ID: mdl-8723652

ABSTRACT

Competitive binding of fluorescent probe 4-(n-dimethylaminostyryl)-1-methylpyiridinium n-toluenesulfonate and lysozyme to liposomes composed of phosphatidylcholine and diphosphatidylglycerol has been investigated. Association constants and binding stoichiometry for probe and protein have been estimated. Increase of the bilayer negative charge was found to be followed by the increase of binding constant and number of phospholipids interacting with lysozyme.


Subject(s)
Fluorescent Dyes/metabolism , Liposomes , Muramidase/metabolism , Pyridinium Compounds/metabolism , Binding, Competitive , Lipid Bilayers
17.
Biofizika ; 41(2): 363-8, 1996.
Article in Russian | MEDLINE | ID: mdl-8723653

ABSTRACT

Using fluorescent probes 1-anilinonaphthalene-8-sulfonate and 4-(n-dimethylaminostyryl)-1-methylpyridinium n-toluenesulfonate the effect of radiation on the properties of liposomes composed of phosphatidylcholine and diphosphatidylglycerol has been investigated. Parameters of the probes association with liposomes were estimated. It was suggested that radiation-induced increase of 1-anilinonaphthalene-8-sulfonate fluorescence intensity and decrease of that for 4-(n-dimethylaminostyryl)-1-methylpyridinium n-toluenesulfonate are caused by lipid's peroxidation.


Subject(s)
Anilino Naphthalenesulfonates/metabolism , Fluorescent Dyes/metabolism , Liposomes , Pyridinium Compounds/metabolism , Radiation Effects , Lipid Peroxidation/radiation effects , Phosphatidylcholines/metabolism , Phosphatidylglycerols/metabolism , Spectrometry, Fluorescence
18.
Biofizika ; 41(2): 348-54, 1996.
Article in Russian | MEDLINE | ID: mdl-8723651

ABSTRACT

Using fluorescent probe 4-(n-dimethylaminostyryl)-1-methylpyridinium n-toluenesulfonate the radiation effect on the structure of liposomes composed of phosphatidylcholine and diphosphatidylgycerol has been investigated. The from of fluorescence spectra was analyzed and inhomogeneous broadening parameters of spectral components were estimated. The polarity of DSM environment and probe distribution between different sites were found to change after irradiation.


Subject(s)
Liposomes , Pyridinium Compounds/metabolism , Phosphatidylcholines/metabolism , Phosphatidylglycerols/metabolism , Spectrometry, Fluorescence
19.
Ukr Biokhim Zh (1978) ; 68(1): 55-60, 1996.
Article in Russian | MEDLINE | ID: mdl-8755102

ABSTRACT

Competitive interaction of fluorescent probe DSM and ribonuclease with liposomes composed of phosphatidylcholine and diphosphatidylglycerol mixtures has been investigated. Parameters of probe and protein binding to lipid bilayer have been estimated.


Subject(s)
Cardiolipins/chemistry , Liposomes/chemistry , Phosphatidylcholines/chemistry , Ribonucleases/chemistry , Binding Sites , Binding, Competitive , Fluorescent Dyes , Lipid Bilayers , Pyridinium Compounds
20.
Biofizika ; 40(2): 389-92, 1995.
Article in Russian | MEDLINE | ID: mdl-7578344

ABSTRACT

Influence of the 5 MeV electron beam on the structural dynamic organization of the protein phase of erythrocyte shadows has been studied by suppression of the tryptophane fluorescence of proteins by acrylamide. It has been observed that the irradiation leads to conformation changes and increase of the structural rigidity of the protein molecules.


Subject(s)
Erythrocyte Membrane/radiation effects , Membrane Proteins/chemistry , Acrylamide , Acrylamides/chemistry , Animals , Cattle , Electrons , Protein Conformation
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