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1.
Biophys Chem ; 298: 107023, 2023 07.
Article in English | MEDLINE | ID: mdl-37148823

ABSTRACT

We have studied by means of small angle neutron scattering and diffraction, and molecular dynamics simulations the effect of lipid membrane fluidity on the amyloid-beta peptide interactions with the membrane. These interactions have been discovered previously to trigger the reorganization of model membranes between unilamellar vesicles and planar membranes (bicelle-like structures) during the lipid phase transition. The morphology changes were taking place in rigid membranes prepared of fully saturated lipids and were proposed to play a role in the onset of amyloid related disorders. We show in this study that the replacement of fully saturated lipids by more fluid mono-unsaturated lipids eliminates the mentioned morphology changes, most likely due to the absence of phase transition within the temperature range investigated. We have therefore controlled the membrane rigidity also while ensuring the presence of membrane phase transition within the biologically relevant temperatures. It was done by the addition of melatonin and/or cholesterol to the initial membranes made of saturated lipids. Small angle neutron scattering experiments performed over a range of cholesterol and melatonin concentrations show their distinctive effects on the local membrane structure only. The cholesterol for example affects the membrane curvature such that spontaneously formed unilamellar vesicles are of much larger sizes than those formed by the neat lipid membranes or membranes with melatonin added. The temperature dependent experiments, however, reveal no influence on the previously discovered membrane breakage whether cholesterol or melatonin have been added.


Subject(s)
Melatonin , Membrane Fluidity , Lipid Bilayers/chemistry , Melatonin/chemistry , Amyloid beta-Peptides/chemistry , Unilamellar Liposomes/chemistry , Cholesterol/chemistry
3.
Dokl Biochem Biophys ; 495(1): 342-346, 2020 Nov.
Article in English | MEDLINE | ID: mdl-33368048

ABSTRACT

This work provides the first characteristics of the rhodopsin SpaR from Sphingomonas paucimobilis, aerobic bacteria associated with opportunistic infections. The sequence analysis of SpaR has shown that this protein has unusual DTS motif which has never reported in rhodopsins from Proteobacteria. We report that SpaR operates as an outward proton pump at low pH; however, proton pumping is almost absent at neutral and alkaline pH. The photocycle of this rhodopsin in detergent micelles slows down with an increase in pH because of longer Schiff base reprotonation. Our results show that the novel microbial ion transporter SpaR of interest both as an object for basic research of membrane proteins and as a promising optogenetic tool.


Subject(s)
Proton Pumps/metabolism , Rhodopsin/metabolism , Rhodopsins, Microbial/metabolism , Sphingomonas/metabolism , Hydrogen-Ion Concentration , Light , Optogenetics/methods , Proton Pumps/genetics , Rhodopsin/genetics , Rhodopsins, Microbial/genetics , Sphingomonas/genetics
4.
Nanoscale Res Lett ; 12(1): 8, 2017 Dec.
Article in English | MEDLINE | ID: mdl-28058641

ABSTRACT

The antitumor activity of pristine C60 fullerene aqueous solution (C60FAS) compared to 5-fluorouracil (5-FU) and pyrrole derivative 1-(4-Cl-benzyl)-3-Cl-4-(CF3-fenylamino)-1H-pyrrol-2.5-dione (MI-1) cytostatic drugs was investigated and analyzed in detail using the model of colorectal cancer induced by 1.2-dimethylhydrazine (DMH) in rats. The number, size, and location of the tumors were measured, and the pathology was examined. It was found that the number of tumors and total lesion area decreased significantly under the action of C60FAS and MI-1. Because these drugs have different mechanisms of action, their simultaneous administration can potentially increase the effectiveness and significantly reduce the side effects of antitumor therapy.

5.
Biochim Biophys Acta Bioenerg ; 1858(4): 318-324, 2017 Apr.
Article in English | MEDLINE | ID: mdl-28131736

ABSTRACT

The structure of phycobiliproteins of the cyanobacterium Acaryochloris marina was investigated in buffer solution at physiological temperatures, i.e. under the same conditions applied in spectroscopic experiments, using small angle neutron scattering. The scattering data of intact phycobiliproteins in buffer solution containing phosphate can be well described using a cylindrical shape with a length of about 225Å and a diameter of approximately 100Å. This finding is qualitatively consistent with earlier electron microscopy studies reporting a rod-like shape of the phycobiliproteins with a length of about 250 (M. Chen et al., FEBS Letters 583, 2009, 2535) or 300Å (J. Marquart et al., FEBS Letters 410, 1997, 428). In contrast, phycobiliproteins dissolved in buffer lacking phosphate revealed a splitting of the rods into cylindrical subunits with a height of 28Å only, but also a pronounced sample aggregation. Complementary small angle neutron and X-ray scattering experiments on phycocyanin suggest that the cylindrical subunits may represent either trimeric phycocyanin or trimeric allophycocyanin. Our findings are in agreement with the assumption that a phycobiliprotein rod with a total height of about 225Å can accommodate seven trimeric phycocyanin subunits and one trimeric allophycocyanin subunit, each of which having a height of about 28Å. The structural information obtained by small angle neutron and X-ray scattering can be used to interpret variations in the low-energy region of the 4.5K absorption spectra of phycobiliproteins dissolved in buffer solutions containing and lacking phosphate, respectively.


Subject(s)
Cyanobacteria/chemistry , Energy Transfer , Scattering, Small Angle , Neutron Diffraction , Phycobiliproteins/chemistry , X-Ray Diffraction
6.
Fiziol Zh (1994) ; 40(3-4): 63-70, 1994.
Article in Ukrainian | MEDLINE | ID: mdl-7621957

ABSTRACT

Damages in the fibrin-formation phase initiated by activation of the blood coagulation system and fibrinolysis and promoted by interaction between fibrinogen and its derivatives (dissolved fibrinogen, products of fibrin and fibrinogen lysis) and by the presence of various blood coagulation inhibitors were found in 34% of practically sound old people and in 47% of people of senile age. It is shown very significant to apply the "ancistrone time" test developed on the basis of enzyme ancistrone-H isolated from the venom of snake Agkistrodon halys halys for estimating the fibrin-formation phase both on the model system and in practically sound people of old and senile age. The ancistrone test permits rapidly (for 30-60s) obtaining qualitative and quantitative characteristic of the fibrinogen level in the blood plasma, of the products of fibrin and fibrinogen lysis, of the blood coagulation inhibitors.


Subject(s)
Crotalid Venoms , Fibrin/analysis , Fibrin/drug effects , Serine Endopeptidases , Aged , Algorithms , Fibrin/biosynthesis , Fibrin Fibrinogen Degradation Products/analysis , Fibrin Fibrinogen Degradation Products/drug effects , Fibrinogen/analysis , Fibrinogen/drug effects , Heparin , Humans , Middle Aged , Reference Values , Thrombin Time , Time Factors
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