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PubMed2006

Evaluation of synthetic polymeric micelles as a stabilization medium for the handling of membrane proteins in pharmaceutical drug discovery.

PURPOSE: Polymeric micelles have been used for solubilization of insoluble drugs and as carriers for drug delivery applications. Here we evaluated an application of the synthetic polymeric micelles in experiments designed to improve the handling and stability of membrane proteins targets. METHODS: Particle sizing by dynamic light scattering was performed in a Zeta Plus Photon Correlation Spectrometer at 532 nm. UGT1A1 activity has been measured in fluorescent assay using scopoletin as a substrate. COX-2 activity has been measured in a fluorescent assay using Amplex Red. Fluorescence Resonance Energy Transfer (FRET) was monitored using either 463 nm excitation wavelength (the emission range 500-600 nm) or 395 nm excitation wavelength (the emission range 500-600 nm). RESULTS: Incorporation of membrane proteins into PreserveX-QML polymeric micelles resulted in improved homogeneity and stability of the preparation and in reduced light scattering. Stabilization of the biological activity of micelle-incorporated membrane proteins, such as the human UGT1A1 and COX-2 both during extended incubations at room temperature and during multiple freeze/thaw cycles, has been achieved. CONCLUSION: PreserveX-QML polymeric micelles help to homogenize and disperse membrane proteins preparations and stabilize the biological activity of the proteins making it more suitable for pharmaceutical assays and applications.

Drug Design↗
PubMed1991

The study of fibrin polymerization with monoclonal antibodies.

Three kinds of monoclonal antibody (Mab) of different specificity have been obtained against the N-terminal disulphide knots of fibrinogen and fibrin. Their effects on different phases of fibrin polymerization have been studied. These antibodies were shown to be directed against different epitopes of the B beta(1-53) fragment of the fibrinogen molecule. The different Mab had different effects both on the rate of protofibril lateral aggregation and on the final turbidity of fibrin clots. The Mab were of three specificities: (1) those from clone 2d-2a inhibited the rate of lateral aggregation of protofibrils and decreased the turbidity of the final clot; (2) those from clone B-4C accelerated the polymerization step but did not affect clot turbidity: and (3) those from clone D-IB did not have any effect on either fibrin polymerization or final clot turbidity. The localization of the epitopes recognized by all three kinds of Mab and analysis of our own data and those of others allow us to conclude that one of the active loci involved in protofibril lateral association is situated in the B beta(15-53) fragment of the fibrinogen molecule. Fibrinopeptide B does not need to be split off for this site to function. Fibrin polymerization can occur when one of the two sites of protofibril lateral aggregation in dimeric fibrin molecules is blocked by Mab, and the final clot turbidity is then reduced. The splitting off of one of the two fibrinopeptides B in fibrinogen molecules by thrombin can take place even when the second B beta(Arg14-Gly15) bond is blocked by an antibody molecule.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1991

Degree of composite resin polymerization with visible light and argon laser.

A study was conducted to compare the degree of resin polymerization achievable using conventional visible light techniques and argon lasing. High performance liquid chromatography was used to extract unpolymerized resin from microfilled and small particle composite resin samples following photoactivation with visible light and the argon laser. It was determined that a significantly greater degree of microfilled resin polymerization was achievable following argon lasing compared to exposure to conventional visible light techniques. Although the small particle composite resin samples were polymerized as well as, or slightly better, with the argon laser, the differences were found to be insignificant. As a result, the argon laser should be considered a potentially advantageous method of initiating the polymerization of dental composite resin restorations.

Argon↗
PubMed1991

[The polymerization shrinkage of light cure composite resin].

The polymerization shrinkage of a number of commercially available composite resin (Starfiil, Durafill, VLC-1 and GD) and an experimental composite #1 which contains 16% DMSOC (a new monomer which expands on polymerization) has been determined using a water-filled dialometer. The results indicated that GD displayed the largest shrinkage value at 2.62 +/- 0.20%, while VLC-1, Durafill and Staifill had smaller values at 2.10 +/- 0.10%, 1.84 +/- 0.20% and 1.42 +/- 0.16%, respectively. The experimental composite. #1 underwent least contraction during setting (0.14 +/- 0.13%). The polymerization shrinkage was influenced by the filler loading and the duration of the exposure to the activating light source. There was little influence of shade of materials on the polymerization shrinkage for VLC-1.

Chemical Phenomena↗
PubMed1991

Actin polymerization promoted by a heptapeptide, an analog of the actin-binding S site on myosin head.

Polymerization of G-actin to F-actin was indicated by an increase in light-scattering intensity after the addition of a heptapeptide (Ile-Arg-Ile-Cys(MT)-Arg-Lys-Gly-OEt), an analog of the actin-binding S-site on S-1 heavy chain. The half-maximal concentration of the heptapeptide which induced an increase in the light-scattering intensity at 25 degrees C was about 110 microM, which was in the range of the dissociation constant of this peptide with F-actin. The polymerization of G-actin to F-actin by binding of the heptapeptide was further demonstrated by ultracentrifugal separation, Pi liberation, and electron microscopy. The polymerization of G-actin was induced only by the heptapeptide, but not by fragments of the heptapeptide. The well known acceleration of polymerization of G-actin by the myosin head may be due to the binding of G-actin with the S-site on the myosin head.

Actins↗
PubMed1990

Relationship among visible light source, composite resin polymerization shrinkage, and hygroscopic expansion.

Composite resins contract during polymerization, and studies have shown that light-cured composite resins shrink toward the polymerizing light source. The purpose of this study was to investigate differences in the adaptation of composite resin to the axial wall in Class V restorations following light curing from the lingual or facial aspects. Polymerization contraction in relation to hygroscopic expansion of the restoration was also investigated. Results showed no statistically significant differences (P less than .05) in the adaptation of composite resin to the axial wall, regardless of the polymerization technique, the composite resin, or the effects of hygroscopic expansion.

Composite Resins↗
PubMed1990

Relationship of sulfation to ongoing chondroitin polymerization during biosynthesis of chondroitin 4-sulfate by microsomal preparations from cultured mouse mastocytoma cells.

A microsomal preparation from chondroitin 4-sulfate-synthesizing cultured mouse mastocytoma cells was incubated with UDP-[3H]GalNAc, UDP-GlcA, and 3'-phosphoadenylylphosphosulfate (PAPS) for 30 s at 10 degrees C and with UDP-[14C]GlcA, UDP-GalNAc, and PAPS for 4 h at 37 degrees C for synthesis of 3H- and 14C-labeled chondroitin/chondroitin sulfate. The latter incubation provided more than 100 times as much product as did the short incubation at 10 degrees C. Upon chromatography of the isolated labeled glycosaminoglycans on a Sepharose CL-6B column, most of the [14C]glycosaminoglycan from the 4 h, 37 degrees C incubation was excluded from the column, indicating that this nascent glycosaminoglycan had been polymerized fully. In contrast, most of the [3H]glycosaminoglycan from the 30 s, 10 degrees C incubation was mostly retarded upon cochromatography on this same column, indicating that the nascent glycosaminoglycan was still growing in size. The labeled fractions representing chondroitin/chondroitin sulfate of varying sizes were analyzed for degree of sulfation by degradation with chondroitin ABC lyase followed by paper electrophoresis of the products. Results indicated that the [14C]chondroitin/chondroitin sulfate formed in the 4-h incubation was 60-70% sulfated. Incomplete chains of [3H]chondroitin/chondroitin sulfate formed in the 30-s incubation were also sulfated as much as 20-25%. As the size of the [3H]chondroitin/chondroitin sulfate increased, there was a concomitant increase in sulfation. These results demonstrate that in this microsomal system sulfation takes place while the nascent chondroitin glycosaminoglycan chains are still actively growing in length, although the sulfation lags somewhat behind the polymerization. This not only indicates a common membrane location for both polymerization and sulfation of chondroitin but also demonstrates that the sulfation of chondroitin by these mastocytoma cells may occur during the process of glycosaminoglycan polymerization rather than subsequent to completion of the glycosaminoglycan chains.

Animals↗
PubMed1990

Is there a relationship between phosphatidylinositol trisphosphate and F-actin polymerization in human neutrophils?

Stimulation of human neutrophils with the chemoattractant N-formyl peptide caused rapid polymerization of F-actin as detected by right angle light scatter and 7-nitrobenz-2-oxa-1,3-diazol (NBD)-phallacidin staining of F-actin. After labeling neutrophils with 32P, exposure to N-formyl peptide induced a fast decrease of phosphatidylinositol 4-bisphosphate (PIP)2, a slow increase of phosphatidic acid, and a rapid rise of phosphatidylinositol 4-trisphosphate (PIP3). Formation of PIP3 as well as actin polymerization was near maximal at 10 s after stimulation. Half-maximal response and PIP3 formation at early time points resulted from stimulation of neutrophils with 0.01 nM N-formyl peptide or occupation of about 200 receptors. Sustained elevation of PIP3, prolonged right angle light scatter response, and F-actin formation required higher concentrations of N-formyl peptide, occupation of thousands of receptors, and high binding rates. When ligand binding was interrupted with an antagonist, F-actin rapidly depolymerized, transient light scatter response recovered immediately, and elevated [32P]PIP3 levels decayed toward initial values. However, recovery of [32P]PIP2 was not influenced by the antagonist. Based on the parallel time courses and dose response of [32P] PIP3, the right angle light scatter response, and F-actin polymerization, PIP3 is more likely than PIP2 to be involved in modulation of actin polymerization and depolymerization in vivo.

Actins↗
PubMed1989

[Relationship between graft polymerization onto model peptide and adhesion of MMA-TBB resin to dentin. Influence of functional monomer].

Graft polymerization of MMA with functional monomers onto silk was carried out to investigate the relationship between the grafting and adhesion of the resin to dentin. Functional monomers did not always promote the graft polymerization onto silk. 4-META, one of the functional monomers, increased the degree of grafting without a conformation change of the silk. Phenyl-P decreased the grafting and also changed the conformation of the silk. On the other hand, these monomers promoted the adhesion of resin to dentin. The graft polymerization of monomers onto collagen was not always necessary for the adhesion of resin to dentin. It was important for the adhesion, that monomers inter-penetrated into the dentin well, and were polymerized in situ.

Acrylic Resins↗
PubMed1989

Cyclic AMP-dependent phosphorylation of glycoprotein Ib inhibits collagen-induced polymerization of actin in platelets.

Platelet function is inhibited by agents such as prostaglandin E1 (PGE1) that elevate the cytoplasmic concentration of cyclic AMP. Inhibition presumably results from the cyclic AMP-stimulated phosphorylation of intracellular proteins. Polypeptides that become phosphorylated are actin-binding protein, P51 (Mr = 51,000), P36 (Mr = 36,000), P24 (Mr = 24,000), and P22 (Mr = 22,000). Recently, we identified P24 as the beta-chain of glycoprotein (GP) Ib, a component of the plasma membrane GP Ib.IX complex. The existence of Bernard-Soulier syndrome, a hereditary disorder in which platelets selectively lack the GP Ib.IX complex, enabled us to examine whether the phosphorylation of GP Ib beta (P24) is responsible for any of the inhibitory effects of elevated cyclic AMP on platelet function. Exposure of control platelets to PGE1 increased phosphorylation of actin-binding protein, P51, P36, GP Ib beta, and P22. Prostaglandin E1 induced the same phosphorylation reactions in Bernard-Soulier platelets, except that of GP Ib beta, which is absent. In control platelets, PGE1 inhibited collagen-induced phosphorylation of myosin light chain, phosphorylation of P47 (an unidentified Mr 47,000 cytoplasmic protein that is phosphorylated by protein kinase C in stimulated platelets), aggregation, and the secretion of granule contents. Despite the absence of GP Ib beta, PGE1 also inhibited these collagen-induced responses in Bernard-Soulier platelets. However, while PGE1 inhibited collagen-induced polymerization of actin in control platelets, it did not inhibit actin polymerization in Bernard-Soulier platelets. These results suggest that cyclic AMP-induced phosphorylation of GP Ib inhibits collagen-induced actin polymerization in platelets. Because actin polymerization is required for at least some of the functional responses of platelets to an agonist, phosphorylation of Gp Ib beta may be one way in which cyclic AMP inhibits platelet function.

Actins↗
PubMed1989

Concentration and degree of polymerization of hyaluronate in equine synovial fluid.

In addition to its well-known physicochemical properties, hyaluronate (HA) has recently been shown to have important biological and pathophysiologic regulatory effects on granulocytes, monocytes, fibroblasts, and endothelial cells, as well as on the healing of wounds and various joint disorders. Many of these effects depend on or are reflected in the concentration and degree of polymerization of HA. Therefore, high-performance liquid chromatography with size-exclusion column was used to characterize the concentration and degree of polymerization of HA in equine synovial fluid (SF). The mean (+/- SD) HA concentration was 0.47 +/- 0.19 mg/ml and there was no difference between control joints and those with positive response to local anesthetic administration (0.61 +/- 0.20 mg/ml vs 0.42 +/- 0.17 mg/ml), suggesting that in horses with acute traumatic synovitis causing lameness, HA concentration in SF cannot be used as a marker for the condition. High-performance liquid chromatograms disclosed considerable variation between horses in the degree of polymerization reflected in the peak area to height ratio (mean +/- SD, 3.207 +/- 0.447; range, 2.229 to 3.915), indicating differences in local synthesis, degradation, or mobilization into lymph of SF HA. In addition, the correlation between SF HA concentration and degree of polymerization was 0.760 (P less than 0.01; linear regression analysis), suggesting that HA concentration and chain length are independently regulated.

Animals↗
PubMed1989

Effects of monomeric and polymeric diets on small intestine following massive resection.

Since the introduction of long-term total parental nutrition, it has been possible to raise the survival rate in patients with massive intestinal resection. How to increase the remaining intestinal mucosa hyperplasia in these patients has become the focus of many studies. Early postoperative enteral feeding with exogenous intraluminal nutrition was considered to be one of the most essential factors. The best enteral food pattern, however, is still not conclusive. In this study, we used the animal model of rats with 60% small intestinal resection, giving them different kinds of enteral diets through gastrostomy tubes. The monomeric diet included amino acid, glucose, disaccharide, and triglyceride. The polymeric diet included the usual source of nutrition such as protein, polysaccharide, and fat. The rats were killed three weeks later. Histopathological changes of the remaining bowel and H3 thymidine incorporation to mucosal DNa were measured. We found: (1) hyperplasia of the remaining bowel in the 60% resected rats was definitely increased more than the rats of the sham operation; (2) from the protein content, the DNA content of mucosa cells, the villus height and crypt depth points of view, the polymeric diet fed rats had a better adaptation; (3) on the 21st postoperative day, the DNA synthetic rate was still very high in polymeric diet fed rats, but returned to preoperative levels in rats fed with a monomeric diet. Our conclusion of this study is that a polymeric diet can contribute to a better intestinal mucosa regeneration than a monomeric diet in the rats with massive intestinal resection.

Adaptation, Physiological↗
PubMed1989

Inhibition of the metastasis of murine malignant melanoma by synthetic polymeric peptides containing core sequences of cell-adhesive molecules.

We investigated that the antimetastatic and antiadhesive activities of peptides based on Arg-Gly-Asp adhesive signal in fibronectin could be augmented by their polymerization. Poly(Arg-Gly-Asp), which consists of a repetitive sequence of Arg-Gly-Asp, inhibited lung metastases in C57BL/6 mice more effectively than Arg-Gly-Asp tripeptide was able to do, when coinjected or separately injected with B16-BL6 cells. The adhesion of tumor cells to fibronectin was specifically inhibited by adding poly(Arg-Gly-Asp) but not unrelated peptides. In contrast, poly(Arg, Gly, Asp), in which three amino acids are randomly arranged, showed neither inhibition of lung metastases nor any adhesive ability to attach to tumor cells. The inhibitory effect of polymeric peptides containing the Arg-Gly-Asp sequence on lung metastases decreased according to the decreasing repeat units of the Arg-Gly-Asp core sequence. Polymeric peptides with Arg-Gly-Asp entrapped within the liposome membranes also caused a remarkable reduction of metastatic colonies. In a spontaneous metastasis model, multiple i.v. administrations of poly(Arg-Gly-Asp) after tumor inoculation caused the significant reduction of metastatic colonies in the lung but did not affect the growth (size) of primary tumor. We found that the polymerization (multivalency) of the Arg-Gly-Asp core sequence was able to augment the inhibition of tumor lung metastases in experimental and spontaneous metastasis models as well as the cell-adhesive property more effectively than a monovalent unit of Arg-Gly-Asp peptide.

Amino Acid Sequence↗
PubMed1989

[Curing ability of polymerization lights for composite materials].

An in-vivo study has been conducted with four different brands of activator light sources. 38 light units in service by different dental practitioners were compared with new light sources. Curing depth profiles were obtained using Knoop microhardness measurements. It was observed that with an exposure time of up to 60 s the polymerization was not sufficient below 2 mm of depth. The "old" light sources showed worse curing properties than the new ones, especially below this depth. Generally, the polymerization units with rigid glass fiber light guide showed better results than the units with a flexible fiber-optic cable. Other reasons for insufficient polymerization were polymerized composite material at the end of the light guide, a defect in the cooling system of the light source and, for two brands of light sources, a reduction of the voltage below 220 V.

Composite Resins↗
PubMed1987

Effect of amino acid at the beta 6 position on surface hydrophobicity, stability, solubility, and the kinetics of polymerization of hemoglobin. Comparisons among Hb A (Glu beta 6), Hb C (Lys beta 6), Hb Machida (Gln beta 6), and Hb S (Val beta 6).

Surface hydrophobicity, stability, solubility, and kinetics of polymerization were studied using hemoglobins with four different amino acids at the beta 6 position: Hb A (Glu beta 6), Hb C (Lys beta 6), Hb Machida (Gln beta 6), and Hb S (Val beta 6). The surface hydrophobicity increased in the order of Hb C, Hb A, Hb Machida, and Hb S, coinciding with the hydrophobicity of the amino acid at the beta 6 position. Solubility of the oxy-form of these hemoglobins decreased in relation to increases in their surface hydrophobicity, suggesting that the solubility is controlled by the strength of hydrophobicity of the amino acid at the beta 6 position. The solubility of the oxy-form of these hemoglobins is always higher than that of the deoxy-form. There is a similar linear relationship between the solubility and surface hydrophobicity among deoxyhemoglobins A, C, and Machida. However, the solubility of deoxy-Hb S deviated significantly from the expected value, indicating that the extremely low solubility of deoxy-Hb S is not directly related to the hydrophobicity of the beta 6 valine. Kinetic studies on the polymerization of deoxy-Hb Machida revealed a distinct delay time prior to polymerization. This confirms our previous hypothesis that beta 6 valine is not responsible for the delay time prior to gelation. The kinetics of the polymerization of 1:1 mixtures of sickle and non-sickle hemoglobins were similar to those of pure Hb S, suggesting that only one of the two beta 6 valines is involved in an intermolecular contact. In mixtures of equal amounts of Hb S and Hb A, Hb C, or Hb Machida, half of the asymmetrical AS, SC, and S-Machida hybrid hemoglobins behaved like Hb S during nucleation, while the other half behaved like the non-sickle hemoglobin.

Drug Stability↗
PubMed1988

Linkages between the effects of taxol, colchicine, and GTP on tubulin polymerization.

A comparative study has been carried out of the effects of taxol on the polymerizations into microtubules of microtubule-associated protein-free tubulin, prepared by the modified Weisenberg procedure, and of the tubulin-colchicine complex into large aggregates. Taxol enhances, to a much greater extent, the stability of microtubules than that of the tubulin-colchicine polymers so that, with highly purified tubulin, assembly into microtubules takes place at 10 degrees C, even in the absence of exogenous GTP. The polymerization of tubulin-colchicine requires both heat and GTP, and the process is reversed by cooling. These results indicate that in both systems polymerization is linked to interactions with taxol and GTP, the interplay of linkage free energies imparting the observed polymer stabilities. In the case of microtubule formation, the linkage free energy provided by taxol binding is approximately -3.0 kcal/mol of alpha-beta-tubulin dimer, whereas this quantity is reduced to approximately -0.5 kcal/mol in tubulin-colchicine, indicating the expenditure of much more binding free energy in the latter case for overcoming unfavorable factors, such as steric hindrance and geometric strain. The difference in the effect of GTP on the two polymerization processes reflects the respective abilities of the bindings of taxol to the two states of tubulin to overcome the loss of the linkage free energy of GTP binding. Analysis of the linkages leads to the conclusions that taxol need not change qualitatively the mechanism of microtubule assembly and that tubulin with the E-site unoccupied by nucleotide should have the capacity to form microtubules, the reaction being extremely weak.

Alkaloids↗
PubMed1985

[Cytochrome c-induced acceleration of the reaction of muscle actin polymerization].

The reaction of rabbit skeletal muscle actin polymerization initiated by the addition of neutral salts is accelerated in the presence of mitochondrial cytochrome c. The observed effect is specific, since the addition of serum albumin does not change the initial velocity of this process. The dependence of the rate of actin polymerization and exogenous cytochrome c concentration correlates within the molar protein ratios from 43:1 to 9:1, respectively. The increase in the polymerization rate occurs immediately after addition of cytochrome c to the reaction mixture; however, the maximal effect is observed only after 5 min coincubation of the proteins. The ability of cytochrome c to stimulate this process is abolished at alkaline values of pH (8.5), which points to the significant role of the molecule positive charge which, in all probability, serves as a primer of the muscle actin polymerization reaction.

Actins↗
PubMedDate not supplied

Adjusting the polymerization time of isobutyl-2 cyanoacrylate.

Isobutyl-2 cyanoacrylate (IBCA) polymerizes by an anionic mechanism. The initiation of polymerization depends on an alkaline medium and can be inhibited with the addition of small amounts of acid. Using small amounts of glacial acetic acid (3.7%-7.1% by volume), the polymerization time was prolonged from 2.3 sec to 7.8 sec. In vivo experiments in dogs demonstrated no additional inflammatory reactions to the mixture of IBCA, iophendylate, and tantalum powder when acetic acid was added. Glacial acetic acid offers a safe and effective way, without increase in viscosity, to manipulate the polymerization time of IBCA.

Acetates↗