Spatial structure of angiotensin in an aqueous solution

The spatial structure of spin-labeled angiotensin in aqueous solution wa investigated with the combined use of NMR, fluorescence spectroscopy and energy calculation including Monte-Carlo techniques. The calculated mean values of molecular parameters were compared with the experimental ones. The calculated and experimental mean values were regarded as statistically indistinguishable when the corresponding mean values occurred within the 95% confidence limit. The experimental parameters were shown to be adequately described by calculated conformers only with the assumption of the existence of dynamic equilibrium of conformers in solution. The mean values of statistical weights and their limits providing the agreement between the calculated and experimental data were determined. Two geometrically different forms of backbone structure for C-terminal hexapeptide in aqueous solution were revealed using the discussed approach; the N-terminal part of the molecule appeared to be much more conformationally labile. The model of molecule spatial structure is consistent with available literature data upon angiotensin titration experiments, its complexing with heavy metal ions etc.     

Crystallization of chondroitin sulfate from an aqueous solution

A new polymorph of sodium chondroitin-4-sulfate has been crystallized from an ethanolic aqueous solution at low pH. The crystallized spherulite specimens give considerably sharper x-ray diffraction lines. The unit cell of the new polymorph is rectangular with dimensions (Å) a = 16.0, b = 24.1, and c = 26.0. The chondroitin-4-sulfate could be purified by recrystallization.     

Lower Photostability of Capsanthin Dispersed in an Aqueous Solution

Food-additive grades of capsanthin, lutein, lycopene, and β-carotene dispersed in aqueous solutions were photo-irradiated using a Xenon weather meter, and the levels of carotenoids were measured by HPLC and the absorbance method. Capsanthin photo-degraded more rapidly than the carotenoids tested, with less oxygen consumption. Unlike carotenes, capsanthin was partially converted into analogous colored compounds during degradation.     

Oligo-glycine synthesis in an aqueous solution of glycine under oxidative conditions

Di-and tri-glycine were synthesized in 1M aqueous solution of glycine by bubbling for 90 hr with oxygen discharged in the path from an oxygen cylinder. The peptides were also produced by an incubation at 37°C of 2M glycine solution prepared with 75% hydrogen peroxide, and the yields were traced for 200 days. The final yields were about 0.25% and 0.01% for di-and tri-glycine, respectively. The solution at 166 days of incubation was applied to a Sephadex G 10 column, and the fractions around the top of the chromatogram were found to increase the intensity of ninhydrin color about 45 times after hydrolysis, indicating an existence of oligo-glycine. The solutions of 1M glycine and 0.5M diglycine prepared with 30% hydrogen peroxide were incubated at 37°C for 38 days, and di-and tetra-glycine were detected in the yields of 0.12% and 0.33%, respectively.     

A model for the simulation of an aqueous dipeptide solution

A model for the simulation of a solution of an alanine dipeptide in water is presented that combines a previous model for bulk water (ST2) with that used in conformational energy studies on small molecules and proteins. The results of a pilot molecular dynamics study indicate that the model leads to reasonable solvent–solute interactions. No evidence is found for substantial changes in the structure or dynamics of the dipeptide in solution as compared to in vacuo. Furthermore, at the elevated temperature examined, there appear to be no significant effects on the dynamics or intermolecular bonding of the water molecules in contact with the solute.     

Molecular dynamics study on an adipokinetic hormone peptide in aqueous solution

Lom-AKH-I is a member of the adipokinetic hormone/red pigment concentrating hormone (AKH/RPCH) family of peptides found in flying insects. A molecular dynamics simulation at room temperature (293 K) in water has been performed to survey the folding path of the Lom-AKH-I peptide in water and to establish the secondary structure of Lom-AKH-I. The obtained results indicate the presence of an undefined extended conformation.     

Heparin-polypeptide interactions in aqueous solution

Circular dichroism spectroscopy has been used to study the interactions between heparin and cationic polypeptides in dilute aqueous solution at neutral pH. The results indicate that poly(l-lysine), poly(l-arginine), and poly(l-ornithine) adopt the α-helical conformation in the presence of heparin, rather than the “charged coil” form observed for the polypeptide alone under the same conditions. Maximum interaction for the poly(l-lysine) and poly(l-ornithine) systems occur at an amino acid: disaccharide residue ratio of 2.3 ± 0.1:1, which correlates with the analytical data of 2.3 sulfates per heparin disaccharide. For poly(l-arginine), maximum interaction occurs at a residue ratio of 3.3 ± 0.1:1, and indicates that all the anionic groups (sulfate and carboxyl) of the heparin are involved in this case.The interactions of heparin are analogous to those observed previously for six connective tissue mucopolysaccharides, except that none of the latter had any effect on the conformation of poly(l-ornithine). The poly(l-ornithine)-heparin system shows a thermal “melting” transition at T_m = 56.0 ± 1.0 °C, at which point the polypeptide reverts to the “charged coil” form; the interactions with poly(l-lysine) and poly(l-arginine) are stable up to temperatures > 90 °C. The high thermal stability of these conformation-directing effects indicate a stronger interaction for heparin than the other mucopolysaccharides, which is probably due to the high sulfate content.     

Trehalose-protein interaction in aqueous solution

A variety of sugars are known to enhance the stability of biomaterials. Trehalose, a nonreducing disaccharide composed of two alpha, alpha(1 --> 1)-linked D-glucopyranose units, appears to be one of the most effective protectants. Both in vivo and in vitro, trehalose protects biostructures such as proteins and membranes from damage due to dehydration, heat, or cold. However, despite the significant amount of experimental data on this disaccharide, no clear picture of the molecular mechanism responsible for its stabilizing properties has emerged yet. Three major hypotheses (water-trehalose hydrogen-bond replacement, coating by a trapped water layer, and mechanical inhibition of the conformational fluctuations) have been proposed to explain the stabilizing effect of trehalose on proteins. To investigate the nature of protein-trehalose-water interactions in solution at the molecular level, two molecular dynamics simulations of the protein lysozyme in solution at room temperature have been carried out, one in the presence (about 0.5 M) and one in the absence of trehalose. The results show that the trehalose molecules cluster and move toward the protein, but neither completely expel water from the protein surface nor form hydrogen bonds with the protein. Furthermore, the coating by trehalose does not significantly reduce the conformational fluctuations of the protein compared to the trehalose-free system. Based on these observations, a model is proposed for the interaction of trehalose molecules with a protein in moderately concentrated solutions, at room temperature and on the nanosecond timescale.     

Changes in the secondary structure of collagen after gamma-irradiation in an aqueous solution

The conformation of calf skin collagen at the secondary structure level changed after 60Co-gamma-radiation with doses ranging from 50 to 1,000 Gy in aerated aqueous solutions and in the presence of N2 and N2O. Despiralization of collagen at a dose of 1,000 Gy reached 90% in N2O, 70% in N2, and 60% in the aerated solution. The radiochemical yield of the despiralized collagen molecules was 0.007 mol/100 eV owing to OH(.). The presence of radioprotective agents upon irradiation of collagen solutions diminished considerably the injury to its secondary structure.     

Oxygen transfer in mechanically agitated aqueous systems containing dispersed hydrocarbon

The effect of dispersed n -dodecane or n -hexadecane on the air-to-aqueous phase overall volumetric oxygen transfer coefficient in a simulated (cell-free) stirred-tank fermentor is described. The oil volume fraction ranged from zero to 0.10; the ionic strength of the aqueous phases was varied from 0 to 0.45. The air-to-aqueous phase coefficients in both oil-free (K_La) and oil-bearing (K_La*) systems were evaluated from unsteady-state experiments using a membrane-covered probe to follow the aqueous phase dissolved oxygen tension. For all systems studied, K_La*/K_La was found to be independent of P/V and v_s for all practical purposes. However, for a particular aqueous phase and at a given P/V and v_s, the ratio K_La*K_La generally differed from unity. Depending on the combination of hydrocarbon type and volume fraction and the aqueous-phase ionic strength employed, the dispersed hydrocarbon may, in some cases, reduce the rate of oxygen transfer and in others enhance it relative to that of the corresponding oil-free gas–liquid dispersion. Enhancement of the air-to-aqueous transfer rate by such negative spreading coefficient hydrocarbons has not been reported previously.     

Conformation of allantoicase in aqueous solution

1. The separation of 0.9-S and 10.8-S allantoicase with the aid of a 2H2O-H2O gradient was described. The resulting preparations were subjected to sedimentation equilibrium, optical rotatory dispersion (ORD), circular dichroism (CD) and infrared studies. 2. The molecular weight of 0.9-S allantoicase was determined to be about 1.1 x 10(4) g/mole in studies on the sedimentation behavior, the metal content and amino acid composition. The molecular weight of 10.8-S allantoicase was about 15.4 x 10(4) g/mole. 3. Optical rotatory dispersion, circular dichroism and infrared studies indicated that both molecules contain alpha-helix, beta conformation and random coil. A Cotton effect at 418 nm was ascribed to the asymmetric binding of Mn2+ to the enzyme. Competitive inhibitors decreased the absorption and circular dichroism bands at about 280 nm and 418 nm. These phenomena suggested that the aromatic groups may play an essential role in the binding of substrates and inhibitors by the Mn(2+)-enzyme complex. 4. Comparison of alpha-helical contents of metalloallantoicases showed that the enzymes with low helical contents exhibited high enzymic activities. 5. The nearly identical physicochemical behavior and specific enzymic activity of 0.9-S and 10.8-S allantoicase indicated that they are very similar in structure and conformation.     

Equilibria of polyoxometalates in aqueous solution

In most aqueous polyoxometalate systems, numerous, often highly negatively charged species, are formed. To establish the speciation in such complex polyanion systems, many experimental methods and techniques must be used. Moreover, it is of vital importance that the experimental data are of the highest accuracy and that the data collected from different methods are treated simultaneously with an appropriate computer program. In systems containing one or more sensitive NMR nuclei, a combined EMF-NMR method has been shown to be extremely powerful.This article firstly gives some general comments on equilibria in aqueous polyoxometalate systems including ionic medium effects, and then describes an equilibrium EMF-NMR (³¹P and⁵¹V) study of the five component system H⁺-Mo(VI)-V(V)-P(V)-e^–. The study has been focused on so-called Keggin ratio solutions, Mo+V):P=12:1, since these are commonly used in selective oxidation processes. Special attention has been given to Mo₁₀V₂P and Mo₉V₃P solutions, where positional isomers occur. We have been able to identify and characterize all the five possible isomers of -Mo₁₀V₂PO ₄₀ ^5– at 25 and 90 °C. Besides the results from the five component system, some interesting findings from the binary, ternary and quarternary sybsystems are also reported.     

Oxidation by superoxide of tocopherols dispersed in aqueous media with deoxycholate

alpha-Tocopherol dispersed in aqueous media with deoxycholate was found to be oxidized, at a physiological pH, by a xanthine-xanthine oxidase system. This reaction was completely inhibited by the addition of superoxide dismutase, whereas catalase and mannitol (scavenger of hydroxyl radical) did not affect the reaction. This finding indicates that the oxidation of alpha-tocopherol is caused by O2. The reaction product formed was identified as 8 alpha-hydroxy-alpha-tocopherone by thin-layer chromatography and ultraviolet spectroscopy. The product was found to change spontaneously to alpha-tocopherol quinone. beta-, gamma-, and delta-tocopherol dispersed with deoxycholate also reacted with O2. The reaction of tocopherols dispersed in the micellar form may be considered as a model of in vivo reaction of tocopherols, since tocopherols are present in tissues largely in the membranes, where O2 is known to be generated.     

Conformation of poly-L-tyrosine in aqueous solution

The conformational transition of poly-L -tyrosine in 0.1M KCl was investigated by ORD and infrared spectroscopy, potentiometric titration, and sedimentation velocity experiments. It is shown that the fully ordered conformer is obtained by slow titration of the random coil with 0.1N HCl at 25°C. The charge-induced transition, at variance with other poly-α-amino acids, is completed in a narrow range of α. An aggregation process was detected both by potentiometric titration and sedimentation velocity. The polyamino acid aggregates around α = 0.7 at 25°C when the conformational transition is almost complete. Infrared spectra, in the region of the amide I band (1650 cm^?1) showed that the transition is a random coil → antiparallel β one. Evidence exists that the form is of the intramolecular type. The foregoing interpretations of ORD and CD spectra in terms of the α-helix conformation are discussed.     

Synthesis of amino-analogs of bacteriochlorophyll-d and their self-aggregation in an aqueous micelle solution

Zinc methyl 3-aminomethyl- and 3-(1-aminoethyl)-pyropheophorbides-a were prepared by modifying naturally occurring chlorophyll-a. The synthetic amino-analogs of bacteriochlorophyll-d self-aggregated in an aqueous micelle solution to give large oligomers with red-shifted and broadened electronic absorption bands. The spectra of these self-aggregates were similar to those of bacteriochlorophyll self-aggregates in the main light-harvesting antennas of green photosynthetic bacteria. The 3¹-amino groups were alternative to the 3¹-hydroxy groups in natural bacteriochlorophylls-c/d/e/f.     

Biosorption of phenol from an aqueous solution by Aspergillus niger biomass

Intra-particle diffusion of sulfuric acid into sugarcane bagasse, corn stover, rice straw and yellow poplar was investigated to determine the effective diffusivity of sulfuric acid within the porous biomass structure. Diffusion experiments were conducted over 25-75 degrees C for two different biomass sizes using dynamic diffusion test cells. Diffusivities of sulfuric acid in agricultural residues were significantly higher than those of hard wood. Diffusivity data for each biomass were fitted into the Arrhenius equation for extrapolation to higher temperatures. The diffusivity data were subsequently incorporated into a theoretical model to determine acid profile within the biomass matrix. The modeling results indicate that intra-particle diffusion of acid influences the rate of dilute-acid pretreatment if unground biomass feedstock is used under normal pretreatment conditions. A criterion was set up to determine the critical biomass size at which the intra-particle acid diffusion becomes a rate-influencing factor for a given pretreatment condition.