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At least 1,153 records · Page 64Linked to original sources
PubMed2000

Light scattering investigations on dilute nonionic oil-in-water microemulsions.

Dilute 3-component nonionic oil-in-water microemulsions formulated with either a polyoxyethylene surfactant (C18:1E10 or C12E10) or the alkylamine-N-oxide surfactant, DDAO (C12AO), and containing either a triglyceride or an ethyl ester oil have been examined using dynamic and static light-scattering techniques. Analysis of the results showed distinct differences in the tested oil's mode of incorporation into the microemulsion droplets, with both the molecular volume of the oil and the hydrophobic chain length of the surfactant being important. For example, microemulsions formulated by C18:1E10 and containing one of the larger molecular volume oils (that is, either a triglyceride, Miglyol 812, or soybean oil) or the ethyl ester of fatty acid oil, ethyl oleate, exhibited first a decrease and then an increase in hydrodynamic size and surfactant aggregation number, suggesting that the asymmetric C18:1E10 micelles became spherical upon the addition of a small amount of oil and grew thereafter because of further oil being incorporated into the core of the spherical microemulsion droplet. A similar conclusion of sphericity could not be drawn for microemulsions stabilized by C18:1E10 and containing one of the oils smaller in molecular volume (namely tributyrin, ethyl butyrate, or ethyl caprylate) where neither the aggregation number nor the hydrodynamic radius changed much upon the addition of oil. This result suggested that these oils were preferentially located in the interfacial surfactant monolayer, behaving in much the same way as a cosurfactant. A different trend of results, however, was seen for microemulsions prepared using C12E10 and C12AO, most likely because these surfactants produced approximately spherical micelles. In this case, the microemulsions containing the oils larger in molecular volume tended to exhibit an increase in surfactant aggregation number and hydrodynamic size, suggesting the growth of spherical micelles, while the smaller oils (in particular ethyl butyrate) caused a significant decrease in surfactant aggregation number incompatible with their being incorporated into the centre of the droplet, suggesting that the oils were being located in the interfacial surfactant monolayer. These results suggest that the various oils are incorporated into the microemulsions in very different ways.

Dimethylamines↗
PubMed1982

Decreased structure-linked latency of lysosomal dipeptidyl aminopeptidase-I activity in Duchenne muscular dystrophy fibroblasts.

Crude lysosomal pellets were prepared from skin fibroblasts grown from patients having Duchenne muscular dystrophy, and from normal controls. Disruption of the lysosomes by nonionic detergents resulted in the expression of latent activity of the enzyme dipeptidyl aminopeptidase-I(DAP-I). Duchenne lysosomes showed less structure-linked latency than those from normal controls, and sedimentation studies demonstrated that the difference was not caused by increased leakage of the enzyme from lysosomes. Permeability properties of the lysosomes for an artificial substrate revealed no difference of the apparent Km. However, in intact lysosomes the apparent K, for Cl- of this chloride-requiring enzyme was found to be lower in DMD lysosomes. The apparent increase in entry for Cl- was closely related with the decreased amount of the DAP-I latency. High concentrations of extra-lysosomal Cl- corrected the abnormality.

Cathepsins↗
PubMed1995

Studies on cognitive enhancing agents. I. Antiamnestic and antihypoxic activities of 2-dimethylaminoethyl ethers and related compounds.

N-(2-Dimethylaminoethyl)carboxamide (1a-d), 2-dimethylaminoethyl alkyl ether (2a, b), and 2-dimethylaminoethyl 2-hydroxy-2-phenethyl ether (3a-c) and its amino and methylene analogues (3d, 4) have been screened for antiamnestic and antihypoxic activities in mice. A clear reversing effect on electroconvulsive shock-induced amnesia was found with 1a-d, 2a,b, and 2-dimethylaminoethyl 2-hydroxy-2-phenylethyl ether (3a). However, a protective effect against hypoxia was only observed with 3a. Compound 3a, which displayed the dual activity, was further investigated for ameliorating effect on CO2-induced memory impairment, and it was found to be more potent than indeloxazine and bifemelane. In addition, the acute toxicity of 3a in mice was significantly lower than that of tacrine, but its serum-to-brain penetration ability in rats was less than that of the reference drugs.

Amnesia↗
PubMed2005

Investigations into biochemical changes of genetic hypertensive rats using 1H nuclear magnetic resonance-based metabonomics.

Genetically hypertensive rats provide a simple and accessible model for studying essential hypertension, which is a polygenic, heterogenous and multifactorial disease. Their genetic and metabolic features are of great interest because they may provide insight into the pathophysiological processes underlying essential hypertension. We have investigated the genetic influence on metabolic balance and metabolite excretion patterns in stroke-prone spontaneously hypertensive rats (SHRSP) with established hypertension using 1H NMR-based metabonomics. Urinary metabolite profiles for SHRSP and their age-matched normotensive controls, Wistar Kyoto rats, were acquired using 1H NMR spectroscopy. Principal components analysis was applied to these complex NMR data to facilitate differentiation and determine metabolic differences between urine samples collected from the hypertensive and normotensive rats. Consequently, it was possible to distinguish urine samples between the two strains in the principal components scores plot. The loadings plot showed that taurine, creatine and some unidentified metabolites resonating at around delta 2.48, 3.10 and 3.58 predominantly contributed to the separation. In SHRSP, the urinary levels of taurine and creatine were found to be higher and the intensities of the unknown signals much lower than those in the Wistar Kyoto rats. Although the pathophysiological significance of these components remains to be elucidated, this study suggests that 1H NMR-based metabonomics is a promising approach to provide new information on metabolic changes related to the pathophysiological processes of the genetically hypertensive rats.

Animals↗
PubMed2005

Self-assembling peptide detergents stabilize isolated photosystem I on a dry surface for an extended time.

We used a class of designed peptide detergents to stabilize photosystem I (PS-I) upon extended drying under N2 on a gold-coated-Ni-NTA glass surface. PS-I is a chlorophyll-containing membrane protein complex that is the primary reducer of ferredoxin and the electron acceptor of plastocyanin. We isolated the complex from the thylakoids of spinach chloroplasts using a chemical detergent. The chlorophyll molecules associated with the PS-I complex provide an intrinsic steady-state emission spectrum between 650 and 800 nm at -196.15 degrees C that reflects the organization of the pigment-protein interactions. In the absence of detergents, a large blue shift of the fluorescence maxima from approximately 735 nm to approximately 685 nm indicates a disruption in light-harvesting subunit organization, thus revealing chlorophyll-protein interactions. The commonly used membrane protein-stabilizing detergents, N-dodecyl-beta-D-maltoside and N-octyl-beta-D-glucoside, only partially stabilized the approximately 735-nm complex with approximately 685-nm spectroscopic shift. However, prior to drying, addition of the peptide detergent acetyl-AAAAAAK at increasing concentration significantly stabilized the PS-I complex. Moreover, in the presence of acetyl-AAAAAAK, the PS-I complex is stable in a dried form at room temperature for at least 3 wk. Another peptide detergent, acetyl-VVVVVVD, also stabilized the complex but to a lesser extent. These observations suggest that the peptide detergents may effectively stabilize membrane proteins in the solid-state. These designed peptide detergents may facilitate the study of diverse types of membrane proteins.

Detergents↗