15 research outputs found
Interactions of the dipeptide paralysin β-Ala-Tyr and the aminoacid Glu with phospholipid bilayers
AbstractExisting evidence points out that the biological activity of β-Ala-Tyr may in part related to its interactions with the cell membranes. For comparative reasons the effects of Glu were also examined using identical techniques and conditions. In order to examine their thermal and dynamic effects on membrane bilayers a combination of DSC, Raman and solid state NMR spectroscopy on DPPC/water model membranes were applied and the results were compared. DSC data showed that Glu perturbs to a greater degree the model membrane compared to β-Ala-Tyr. Thus, alteration of the phase transition temperature and half width of the peaks, abolishment of the pretransition and influence on the enthalpy of the phase transition were more pronounced in the Glu loaded bilayers. Raman spectroscopy showed that incorporation of Glu in DPPC/water bilayers increased the order in the bilayers in contrast to the effect of the dipeptide. Several structural and dynamical properties of the DPPC multilamellar bilayers with and without the dipeptide or Glu were compared using high resolution C-13 MAS (Magic Angle Spinning) spectra and spectral simulations of inhomogeneously broadened, stationary P-31 NMR lineshapes measured under CP (Cross-polarization) conditions. These methods revealed that the aminoacid Glu binds in the close realm of the phosphate in the hydrophilic headgroup of DPPC while β-Ala-Tyr is located more deeply inside the hydrophobic zone of the bilayer. The P-31 NMR simulations indicated restricted fast rotary motion of the phospholipids about their long axes in the organized bilayer structure. Finally, by the applied methodologies it is concluded that the two molecules under study exert dissimilar thermal and dynamic effects on lipid bilayers, the Glu improving significantly the packing of the lipids in contrast to the smaller and opposite effect of the dipeptide
The LAM-1 band in the low-frequency Raman spectra of even and odd monosubstituted n-alkanes
Conformational properties and interaction of the toxin paralysin β-Ala-Tyr and glu with phospholipids bilayers
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Micellar and surface properties of a poly(methyl methacrylate)–block–poly(N-isopropylacrylamide) copolymer in aqueous solution
Critical micelle concentrations (cmc) of aqueous solutions of poly(methyl methacrylate)–block–poly(N-isopropylacrylamide) were determined at several temperatures by surface tensiometry. Below the lower critical solution temperature (LCST), the low ΔmicH0 determined can be assigned to the PMMA block being tightly coiled in the dispersed molecular state, so that the unfavorable interactions of hydrophobic entities with water are minimized. Above the LCST the cmc value was found to increase; an anomalous behavior that can be directly related to the micelle–globule transition of the hydrophilic block. Interestingly, above the LCST the surface tension of relatively concentrated solutions was found to depend weakly on temperature not following the usual strong decrease with temperature expected for aqueous solutions
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Interactions of Bovine Serum Albumin with Ethylene Oxide/Butylene Oxide Copolymers in Aqueous Solution
The interactions of bovine serum albumin (BSA) with three ethylene oxide/butylene oxide (E/B) copolymers having different block lengths and varying molecular architectures is examined in this study in aqueous solutions. Dynamic light scattering (DLS) indicates the absence of BSA−polymer binding in micellar systems of copolymers with lengthy hydrophilic blocks. On the contrary, stable protein−polymer aggregates were observed in the case of E18B10 block copolymer. Results from DLS and SAXS suggest the dissociation of E/B copolymer micelles in the presence of protein and the absorption of polymer chains to BSA surface. At high protein loadings, bound BSA adopts a more compact conformation in solution. The secondary structure of the protein remains essentially unaffected even at high polymer concentrations. Raman spectroscopy was used to give insight to the configurations of the bound molecules in concentrated solutions. In the vicinity of the critical gel concentration of E18B10 introduction of BSA can dramatically modify the phase diagram, inducing a gel−sol–gel transition. The overall picture of the interaction diagram of the E18B10−BSA reflects the shrinkage of the suspended particles due to destabilization of micelles induced by BSA and the gelator nature of the globular protein. SAXS and rheology were used to further characterize the structure and flow behavior of the polymer−protein hybrid gels and sols
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Polymer − surfactant vesicular complexes in aqueous medium
The introduction of ionic single-tailed surfactants to aqueous solutions of EO18BO10 [EO = poly(ethylene oxide), BO = poly(1,2-butylene oxide), subscripts denote the number of repeating units] leads to the formation of vesicles, as probed by laser scanning confocal microscopy. Dynamic light scattering showed that the dimensions of these aggregates at early stages of development do not depend on the sign of the surfactant head group charge. Small-angle X-ray scattering (SAXS) analysis indicated the coexistence of smaller micelles of different sizes and varying polymer content in solution. In strong contrast to the dramatic increase of size of dispersed particles induced by surfactants in dilute solution, the d-spacing of corresponding mesophases reduces monotonically upon increasing surfactant loading. This effect points to the suppression of vesicles as a consequence of increasing ionic strength in concentrated solutions. Maximum enhancements of storage modulus and thermal stability of hybrid gels take place at different compositions, indicating a delicate balance between the number and size of polymer-poor aggregates (population increases with surfactant loading) and the number and size of polymer−surfactant complexes (number and size decrease in high surfactant concentrations)
Aqueous solutions and gels of diblock copolymers of 1,2-butylene oxide and ethylene oxide studied by light scattering and rheology
Copolymers B20E430, B20E510, and B20E610 (B = oxybutylene repeat unit, E = oxyethylene repeat unit, subscripts indicate chain length in repeat units) were synthesized and characterized by gel permeation chromatography (for distribution width) and 13C NMR spectroscopy (for absolute molar mass and composition). Dynamic and static light scattering were used to determine micellar properties in dilute aqueous solution:  e.g., micelle association numbers and radii. A tube-inversion method was used to define the mobile−immobile (hard gel) phase boundary. For copolymer B20E610, immobile gels form at concentrations as low as 2.9 wt %. Rheological measurements of dynamic modulus and yield stress served to characterize the gel properties and to confirm the phase boundaries. The results are combined with those from previous work on related block copolymers to obtain scaling relationships for the dependence of micellar and gel properties on E-block length, thus enabling prediction of the requirements for and properties of very dilute aqueous gels. The validity of treating the micelles as hard spheres is discussed