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At least 55 records · Page 3Linked to original sources
PubMed1990

Suspension polymerization of 2-hydroxyethyl methacrylate in the presence of polymeric diluents: a novel route to spherical highly porous beads for biomedical applications.

Spherical, highly porous beads of poly(2-hydroxyethyl methacrylate) (PHEMA) cross-linked with ethylene glycol dimethacrylate (EGDM) were prepared by suspension polymerization of HEMA in concentrated NaCl solutions in presence of toluene, poly(methyl methacrylate) (PMMA) in toluene, and poly(tetramethylene glycol) (PTMG). Magnesium hydroxide prepared in situ in the dispersion medium gave the best stabilization effect for the monomer droplets. In the presence of PTMG, beads having nearly 1.0 mm in diameter could be prepared, while toluene alone as the diluent produced beads of very small size. Removal of PMMA or PTMG from the beads after polymerization using suitable solvents gave rise to highly porous PHEMA microspsheres. Polymerization in the presence of PTMG produced microspsheres with better spherical geometry as compared to those generated in the presence of PMMA. The effect of various factors such as NaCl concentration, concentration of Mg(OH)2, and the concentration of PMMA or PTMG in the monomer phase on the stability of the suspension and the particle size distribution was investigated.

Cross-Linking Reagents↗
PubMed1986

Kinetics of sickle hemoglobin polymerization. III. Nucleation rates determined from stochastic fluctuations in polymerization progress curves.

The polymerization kinetics of sickle cell hemoglobin are found to exhibit stochastic variations when observed in very small volumes (approximately 10(-10) cm3). The distribution of progress curves has been measured at several temperatures for a 4.50 mM-hemoglobin S sample using a laser-photolysis, light-scattering technique. The progress curves at a given temperature are superimposable when translated along the time axis, showing that the variability of the kinetic progress curves results primarily from fluctuations in the time at which polymerization is initiated. The shapes of the initial part of the progress curves are well-fitted using the functional form I(t) = Io + As exp (Bt), derived from a dual nucleation model. When the distribution of the measured tenth times is broad, the rate of homogeneous nucleation can be obtained by fitting the exponential tail of the distribution. As the distribution sharpen, the rate of homogeneous nucleation can be estimated by modelling the width of the distribution function using a simple Monte-Carlo simulation of the polymerization kinetics. Using the rates of homogeneous nucleation obtained from the distributions, the rates of heterogeneous nucleation and polymer growth can be obtained from the experimental parameters As and B. The resulting nucleation rates are roughly 1000 times greater than those obtained from an analysis of bulk kinetic data. The results provide strong support for the dual-nucleation mechanism and show that the distribution of progress curves provides a powerful independent method for measuring the rate of homogeneous nucleation and thereby obtaining values for the other principal rates of the mechanism.

Hemoglobin, Sickle↗
PubMed2000

Carbohydrate/monomer complexes in aqueous polymerizations: methylated-beta-cyclodextrin mediated aqueous polymerization of hydrophobic methacrylic monomers.

Hydrophobic methacrylic monomers were polymerized in aqueous media using methylated (1.8)-beta-cyclodextrin (MeCD) additives. Hydrophobic monomers tert-butyl methacrylate (tBuMA), cyclohexyl methacrylate (CMA), and 2-ethylhexyl methacrylate (2EHMA) were each dissolved in chloroform with MeCD. Chloroform was then evaporated to yield solid monomer/cyclodextrin complexes. Complexes were shown by 1H NMR and thermogravimetric analysis (TGA) to have molar ratios of monomer to MeCD as high as 0.72/1.00. The water-soluble complexes were readily polymerized in aqueous media using free radical initiation. During polymerization, hydrophobic methacrylic polymers precipitated and the majority of MeCD remained in solution. Poly(alkyl methacrylates) synthesized via this method exhibited number-average molecular weights ranging from 50,000 to 150,000 with polydispersities from 3.2 to 5.5 depending on monomer structure, and isolated yields were as high as 86%. Additionally, corresponding methacrylic/carbohydrate films were prepared and examined. High molecular weight poly(tBuMA), poly(CMA), and poly(2EHMA) were blended with MeCD to produce optically clear films with as high as 20 wt % MeCD. Differential scanning calorimetry (DSC) characterization indicated that the glass transition temperatures of these novel carbohydrate blends were controllable over a 20 degrees C range depending on the relative concentration of each component.

Carbohydrates↗
PubMed1981

Fibrin Polymerization. 1. Alkylating peptide inhibitors of fibrin polymerization.

A series of analogues relating to the NH2-terminal region of the fibrin alpha chain, i.e., Gly-Pro-Arg-Pro, were prepared by stepwise solid-phase synthesis, and their abilities to inhibit fibrin polymerization and to prolong thrombin-initiated clotting time were evaluated. Among the analogues systematically modified at different positions, replacement of the NH2-terminal three residues of Gly-Pro-Arg-Pro by either chlorambucil, p-nitrophenyl-L-alanine, or p-aminophenyl-L-alanine gave inactive compounds in the thrombin time assay, whereas similar substitution or extension of the COOH terminus produced the highly active analogues Gly-Pro-Arg-Phe(4-NH2), 22%; Gly-Pro-Arg-Pro-Phe(4-NO2), and Gly-Pro-Arg-Pro-Phe(4-NH2), 105%; relative to Gly-Pro-Arg-Pro = 100% in the fibrin polymerization inhibitory assay. As potential photoaffinity labeling probes, analogues containing a nitrophenylalanine residue in position 4 or 5 underwent photolysis under the experimental photoactivation conditions. As a potential alkylating probe, Chl-Pro-Arg-Pro was selectively effective in inhibiting thrombin amidolysis and fibrin polymerization. In the latter assay, Chl-Pro-Arg-Pro was approximately 20 times more potent than Gly-Pro-Arg-Pro in inhibiting fibrin aggregation.

Alkylation↗
PubMed1998

Semicrystalline Polymers via Ring-Opening Polymerization: Preparation and Polymerization of Alkylene Phthalate Cyclic Oligomers.

Preparation of cyclic oligomeric alkylene phthalates via pseudo-high dilution condensation of alkylene diols with iso- and terephthaloyl chlorides and conversion to high molecular weight polyesters via ring-opening polymerization is described. Sterically unhindered amines such as quinuclidine or 1,4-diazabicyclo[2.2.2]octane (DABCO) catalyze the condensation significantly faster than other tertiary amines and are useful for carrying out this conversion in high yield, in the first direct reaction of diol and diacid chloride to form cyclic polyesters. The mixtures of oligomeric cyclics melt at 150-200 degrees C, providing liquids of low viscosity. Ring-opening polymerization using tin or titanate catalysts affords high molecular weight polymers within minutes. Complete polymerization of PBT oligomeric cyclics can be achieved at 180-200 degreesC, significantly below the polymer's melting point of 225 degreesC, and with molecular weights as high as 445 x 10(3). Polymers formed via such a process are more crystalline than conventionally prepared polyesters.

Journal Article↗
PubMed1983

Network formation by neurofilament-induced polymerization of tubulin: 200K subunit of neurofilament triplet promotes nucleation of tubulin polymerization and enhances microtubule assembly.

The previous paper (Minami, Y., et al. (1982) J. Biochem. 92, 889-898) demonstrated that the neurofilament preparation obtained from porcine brain promotes tubulin polymerization, thereby leading to network formation in vitro. Since this preparation fractionated by gel filtration and centrifugation was contaminated mainly by tubulin, the neurofilaments thus prepared were solubilized in a 6 M urea solution, further purified by hydroxyapatite column chromatography, and reconstituted into neurofilaments. This highly purified neurofilament was found to retain the ability to stimulate microtubule assembly and to cause gelation. Next we separated the purified neurofilament into the individual triplet subunits, referred to as 200K, 150K, and 70K proteins, by DEAE-cellulose (DE-52) column chromatography in the presence of 6 M urea. By measuring viscosity and turbidity changes, it has been found that the activity to stimulate polymerization of tubulin is due to the 200K polypeptide, while the 150K protein was less active to promote tubulin polymerization and the 70K protein was totally inactive.

Animals↗
PubMed1998

Mechanochemical solid-state polymerization. IX. Theoretical analysis of rate of drug release from powdered polymeric prodrugs in a heterogeneous system.

We theoretically derived the rate equation of drug release from a simple model in a heterogeneous system. Four assumptions were used to simplify the model. Two kinds of rate equations for drug release derived from two possible limiting cases, that the rate-determining step is a diffusion or hydrolysis controlled process, can predict the experimental results up to 50% hydrolysis. However, the predictions at the later stage by these equations are insufficient. These results suggest that the process of drug release from powdered polymeric prodrugs in a heterogeneous system must be described by both diffusion and hydrolysis. The rate equation derived from a model considering both the diffusion and hydrolysis processes can successfully predict the experimental results for several kinds of polymeric prodrugs. It is also shown that the diffusion coefficient and rate constant for hydrolysis calculated from this equation thoroughly express the character of the comonomer. The rate equation derived from the model that considers both diffusion and hydrolysis is very useful to analyze drug release from various kinds of polymeric prodrugs in a heterogeneous system.

Hydrolysis↗
PubMed2002

[Molecularly imprinted polymeric microspheres prepared by seed swelling and suspension polymerization].

A series of molecularly imprinted polymeric microspheres(MIPMs) were prepared by seed swelling and suspension polymerization method in aqueous system using tyrosine as printing molecules, methacrylic acid as functional monomers and trimethylolpropane trimethacrylate (TRIM) as cross-linkers. The morphology including the size, size distribution, pore and pore distribution of the polymer beads was analyzed by scanning electron microscope(SEM). The major factors that influence these properties of the beads are discussed. The molecule selecting property of the MIPMs was detected through liquid chromatography. The results showed that uniform-sized spherical MIPMs had been prepared in aqueous system by seed swelling and suspension polymerization method, and its surface was distributed with pores between 1 micron to 10 microns. The average bead size was adjusted from about 50 microns to 400 microns by changing the stirring speed and the amount of seeds used during the preparation. The prepared MIPMs exhibited a considerable tendency to adsorb tyrosine, the printing molecules selectively, and the separation factor was up to 1.82 when phenylalanine was chosen as the competitive molecules.

Binding, Competitive↗
PubMed1984

Actin polymerization. The effect of brevin on filament size and rate of polymerization.

Fluorescent probes covalently bound to actin or to the actin binding protein, brevin, have been utilized to provide information about actin filaments formed in the presence of brevin as well as about the effect of brevin on the rate of polymerization. At actin to brevin ratios of 10:1 to 100:1, the observed diffusion coefficients of filaments, as measured by fluorescence photobleaching recovery using rhodamine-labeled actin or fluorescein-labeled brevin, are similar to those calculated from theoretical considerations for rigid rods. At lower brevin concentrations, the observed diffusion coefficients for actin filaments are lower than predicted, indicating that the filament structure is closer to that observed in the absence of brevin where filaments are immobilized due to interactions between them. The fluorescein-labeled brevin was found to be about as effective in influencing actin polymerization as unlabeled brevin. Using pyrene-labeled actin, we show that brevin binds 2 mol of monomeric actin. We conclude that at sufficiently high brevin concentration there is one brevin molecule per actin filament. From measurements of the initial rate of polymerization at 5.9 microM actin in the presence of brevin, we calculate both the apparent elongation rate constant and dissociation rate constant from one end (presumably the slow-growing end) of the actin filament. The former is highly dependent on Mg2+ concentration while the latter is not.

Actins↗
PubMed1998

In vivo stimulation of polymeric Ig receptor transcytosis by circulating polymeric IgA in rat liver.

Binding of human polymeric IgA ligand to its epithelial cell polymeric Ig receptor, pIgR, has been shown to stimulate pIgR apical transcytosis in an in vitro system, based on polarized confluent MDCK cells expressing rabbit pIgR. The present study aimed at testing whether such a stimulation also occurs in vivo. Transcytosis of pIgR was monitored by rat liver output of total secretory component (SC) into bile, measured by radial immunodiffusion as the sum of free SC and pIgA-bound SC. Whereas in the perfused rat liver system addition of pIgA to the perfusate showed no effect, i.v. injection of human and rat pIgA, but not of monomeric IgA nor PBS, in living rats significantly increased total bile SC output for more than 1 h. Furthermore, depletion of the normal pIgA level circulating in the liver before injecting more pIgA was not required to show the stimulation. Our data thus strongly suggest that stimulation of liver pIgR transcytosis by pIgA ligand binding is physiologically relevant, helping to quickly adjust pIgA transport into bile to increase circulating pIgA levels, without need for increased SC/pIgR synthesis.

Animals↗
PubMed2003

Synthesis and characterization of C13 to C18 stationary phases by monomeric, solution polymerized, and surface polymerized approaches.

A series of bonded phases were synthesized from consecutive length alkylsilanes ranging from C13 through C18, with three different bonding chemistries (monomeric, solution polymerized, and surface polymerized) at each phase length. The phases were characterized in terms of methylene selectivity, shape selectivity, and band broadening. No significant chromatographic differences were found to result from the synthetic routes, except that the different bonding chemistries provide a different range of bonding densities. For bonding densities ranging from 2 to 8 micromol/m2, a linear increase in methylene selectivity was observed with increasing bonding density. Over the narrow range of bonded phase lengths investigated, shape selectivity is more dependent on density than phase length.

Polymers↗
PubMed1997

Polymerization shrinkage and polymerization shrinkage stress in polymer-based restoratives.

OBJECTIVES: This paper is intended to contribute to the recognition and understanding of problems related to polymerization shrinkage. DATA SOURCES: Scientific publications of relevance with regard to this subject were critically reviewed. STUDY SELECTION: The dimensional changes which develop during the curing of resin composites and glass polyalkenoate cements are studied, with special reference to methods of determining shrinkage, shrinkage stress and stress relief. CONCLUSIONS: As no method for handling the adhesive restorative materials has yet been described which guarantees a leakproof restoration, the practitioner has to accept the problem of polymerization shrinkage and destructive shrinkage stress. Only a proper understanding of the mechanisms that cause these problems and the techniques that may reduce their effects will enable the practitioner to derive maximum benefit from the application of resin composites and glass polyalkenoate cements in restorative dentistry.

Composite Resins↗
PubMed2000

Synthesis, characterization, and polymerization activity of [bis(4,4'-bis(neophyldimethylsilylmethyl)-2,2'-bipyridyl)copper(I)]+CuBr2- and Implications for copper(I) catalyst structures in atom transfer radical polymerization.

A series of 4,4'-disilyl-substituted-2,2'-bipyridine ligands were prepared using a metathesis reaction of the dianion of 4,4'-dimethyl-2,2'-bipyridine with several trialkylsilyl chlorides: 4,4'bis(tert-butyldimethylsilylmethyl)-2,2'-bipyridine (dTBDMSbipy), 4,4'-bis(dimethylthexylsilylmethyl)-2,2'-bipyridine (dTHEXbipy), and 4,4'-bis(neophyldimethylsilylmethyl)-2-2'-bipyridine (dNEObipy). It was observed that the side chain length correlated with the ability of the ligand to form hydrocarbon soluble complexes of copper(I) bromide, with dNEObipy forming the most soluble and easily crystallized complexes. The atom transfer radical polymerization (ATRP) of styrene using dNEObipy as the ligand displayed molecular weight control equivalent to other ATRP systems in which solubilizing ligands, such as 4,4'-di-5-nonyl-2,2'-bipyridine or 4,4'-di-n-heptyl-2,2'-bipyridine, were used. The one-to-one complex of dNEObipy with CuBr was prepared and its crystal structure was determined. The resulting complex had the ionic formulation [(dNEObipy)2Cu]+[CuBr2]- and displayed similar activities in styrene ATRP as the standard 2 dNEObipy/CuBr catalyst system. These and other polymerization results in addition to NMR experiments suggest that the predominant copper(I) species formed in ATRP solutions is the 2-to-1 ligand-to-copper(I) cation, [(dNEObipy)2Cu]+, with either a dihalocuprate or halide counteranion, depending upon the conditions.

Journal Article↗
PubMed2002

First example of N-heterocyclic carbenes as catalysts for living polymerization: organocatalytic ring-opening polymerization of cyclic esters.

A novel metal-free, organocatalytic approach to living polymerization is presented. N-heterocyclic carbenes were employed as nucleophilic catalysts for the ring-opening polymerization (ROP) of cyclic ester monomers. The catalysts is used in combination with an initiator, such as an alcohol, which generates an alpha-end group bearing the ester from the initiating alcohol upon ring-opening and a hydroxyl functional omega-chain end that propagates the chain. This class of catalyst proved to be more reactive than tertiary amine and phosphine nucleophiles, producing narrowly dispersed polymers of predictable molecular weights at room temperature in 1-2 h. Catalysis with respect to both initiating alcohol and monomer was observed. Control of the alpha and omega end-groups was demonstrated with a pyrene-labeled initiator, allowing the preparation of well-defined macromolecular architectures. Analogous to the ROP of cyclic esters using biocatalysts, the polymeriztion pathway using the N-heterocyclic carbenes is believed to ensue through a monomer-activated mechanism.

Caproates↗
PubMed2002

Polymeric nanogels produced via inverse microemulsion polymerization as potential gene and antisense delivery agents.

Polymeric nanogel vectors were developed for cellular gene and antisense delivery. Inverse microemulsion polymerization was utilized to synthesize biocompatible nanogels with controlled size, morphology, and composition. The chemical composition, size, polydispersity, stability, and swelling behavior of the nanogels were investigated by NMR, light scattering, transmission electron microscopy, and atomic force microscopy. The cell viability, uptake, and physical stability of nanogel-DNA complexes were evaluated under physiological conditions. Monodisperse nonionic and cationic nanogels were produced with controllable sizes ranging from 40 to 200 nm in diameter. The nanogels demonstrated extended stability in aqueous media and exhibited low toxicity in cell culture. Cationic nanogels formed monodisperse complexes with oligonucleotides and showed enhanced oligonucleotide uptake in cell culture. The nanogels synthesized in this study demonstrate potential utility as carriers of oligonucleotides and DNA for antisense and gene delivery.

Acrylates↗
PubMed2003

Solventless polymerization: spatial migration of a catalyst to form polymeric thin films in microchannels.

This paper reports a simple, additive process to generate patterned polymer films without using any solvent. This process involves a highly efficient catalyst, a Grubbs's catalyst, and a volatile monomer, norbornene. The catalyst and monomers have higher local concentrations inside the microchannels, formed by contacting poly(dimethylsiloxane) stamps to a solid surface, and allow the polymeric thin films to be defined by the microchannels. The patterned thin film serves as an excellent resistant to reactive ion etching, which promises that this process is a complementary, useful alternative to spin-coating and plasma polymerization in microfabrication.

Journal Article↗
PubMed1992

Thrombin promotes actin polymerization in U937 human monocyte-macrophage cells. Analysis of the signalling mechanisms mediating actin polymerization.

The U937 human monocyte-macrophage cell line was used to examine the effect of thrombin, an ill-defined chemoattractant, on the polymerization of actin, a process essential for cell motility. In differentiated macrophage-like U937 cells, thrombin (0.5-50 units/ml) caused a rapid dose-dependent increase in the formation of filamentous (F-) actin, detected by the staining of F-actin with the fluorescent toxin, 7-nitrobenz-2-oxa-1,3-diazole-phallacidin. In contrast with other chemoattractants such as N-formylmethionyl-leucylphenylalanine or C5a, actin polymerization in response to thrombin occurred via a pertussis-toxin-insensitive G1-(inhibitory G-protein) independent signalling pathway. Further, this response was not affected by the Ca2+ chelator EGTA or by the specific protein kinase C (PKC) inhibitor RO-31-8220. The response to thrombin was not mimicked by the Ca2+ ionophore ionomycin or by the direct PKC activator phorbol 12-myristate 13-acetate. The thrombin response was, however, inhibited by the non-specific protein kinase inhibitor staurosporine. The present results suggest that in U937 cells thrombin stimulates the formation of F-actin via a signalling pathway independent of (i) the activation of PKC, (ii) the mobilization of intracellular Ca2+ and (iii) the activation of Ca(2+)-dependent protein kinases, but dependent on the activation of an undefined staurosporine-sensitive protein kinase.

Actins↗
PubMed1983

A rat monoclonal antibody reacting specifically with the tyrosylated form of alpha-tubulin. I. Biochemical characterization, effects on microtubule polymerization in vitro, and microtubule polymerization and organization in vivo.

The antigenic site recognized by a rat monoclonal antibody (clone YL 1/2) reacting with alpha-tubulin (Kilmartin, J.V., B. Wright, and C. Milstein, 1982, J. Cell Biol., 93:576-582) has been determined and partially characterized. YL 1/2 reacts specifically with the tyrosylated form of brain alpha-tubulin from different mammalian species. YL 1/2 reacts with the synthetic peptide Gly-(Glu)3-Gly-(Glu)2-Tyr, corresponding to the carboxyterminal amino acid sequence of tyrosylated alpha-tubulin, but does not react with Gly-(Glu)3-Gly-(Glu)2, the constituent peptide of detyrosylated alpha-tubulin. Electron microscopy as well as direct and indirect immunofluorescence microscopy shows that YL 1/2 binds to the surface of microtubules polymerized in vitro and in vivo. Further in vitro studies show that the antibody has no effect on the rate and extent of microtubule polymerization, the stability of microtubules, and the incorporation of the microtubule-associated proteins (MAP2) and tau into microtubules. In vivo studies using Swiss 3T3 fibroblasts injected with YL 1/2 show that; when injected at low concentration (2 mg IgG/ml in the injection solution), the antibody binds to microtubules without changing their distribution in the cytoplasm. Injection of larger concentration of YL 1/2 (6 mg IgG/ml) induces the formation of microtubule bundles, and still higher concentrations cause the aggregation of microtubule bundles around the nucleus (greater than 12 mg IgG/ml).

Animals↗