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PubMedDate not supplied

Cascade synthesis of chiral block copolymers combining lipase catalyzed ring opening polymerization and atom transfer radical polymerization.

The enantioselective polymerization of methyl-substituted epsilon-caprolactones using Novozym 435 as the catalyst was investigated. All substituted monomers could be polymerized except 6-methyl-epsilon-caprolactone (6-MeCL), which failed to propagate after ring opening. Interestingly, an odd-even effect in the enantiopreference of differently substituted monomers was observed. The combination of 4-methyl-epsilon-caprolactone with Novozym 435 showed good enantioselectivity also in bulk polymerization and resulted in enantiomerically enriched P((S)-4-MeCL) (eep up to 0.88). Subsequently, a novel initiator combining a primary alcohol to initiate the ring opening polymerization and a tertiary bromide to initiate atom transfer controlled radical polymerization (ATRP) was synthesized, and showed high initiator efficiencies (> 90%) in the ring opening polymerization of 4-methyl-epsilon-caprolactone in bulk. In addition, the enantioselectivity was retained (E = 11). By using Ni(PPh3)2Br2 as the ATRP catalyst, Novozym 435 could be effectively inhibited at the desired conversion of 4-methyl-epsilon-caprolactone, thus ensuring a high enantiomeric excess in the polymer backbone. At the same time, Ni(PPh3)2Br2 catalyzed the ATRP of methyl methacrylate resulting in the formation of P((S)-4-MeCL-b-MMA) block copolymers. By this combination of two inherently different polymerization reactions, chiral P((S)-4-MeCL-b-MMA) block copolymers can be conveniently obtained in one pot without intermediate workup.

Catalysis↗
PubMed2005

Single-site anionic polymerization. Monomeric ester enolaluminate propagator synthesis, molecular structure, and polymerization mechanism.

The synthesis and molecular structure of the first examples of monomeric lithium ester enolaluminates that serve as structural models for single-site anionic propagating centers, as well as the mechanism of their polymerization of methacrylates catalyzed by conjugate organoaluminum Lewis acids, are reported. Reactions of isopropyl alpha-lithioisobutyrate (2) with suitable deaggregating and stabilizing organoaluminum compounds such as MeAl(BHT)2 (BHT = 2,6-di-tert-butyl-4-methylphenolate) in hydrocarbons cleanly generate lithium ester enolaluminate complexes such as Li+[Me2C=C(OiPr)OAlMe(BHT)2]- (3). Remarkably, complex 3 is isolable and exists as a monomer in both solid and solution states. Unlike the uncontrolled polymerization of methacrylates by the aggregating enolate 2, the methacrylate polymerization by the monomeric 3 is controlled but exhibits low activity. However, the well controlled and highly active polymerization can be achieved by using the 3/MeAl(BHT)2 propagator/catalyst pair, which is conveniently generated by in situ mixing of 2 with 2 equiv of MeAl(BHT)2. The structure of the added organoaluminum compounds has marked effects on the degree of monomer activation, enolaluminate formation and reactivity, and polymerization control. Kinetics of the polymerization by the 3/MeAl(BHT)2 pair suggest a bimolecular, activated-monomer anionic polymerization mechanism via single-site ester enolaluminate propagating centers. The molecular structures of activated monomer 1, aggregated initiator 2, and monomeric propagator 3 have been determined by X-ray diffraction studies.

Journal Article↗
PubMed2002

Effect of polymerization under pressure on indirect tensile mechanical properties of light-polymerized composites.

STATEMENT OF PROBLEM: Flaws developed during polymerization of restorative materials cause a decrease in mechanical properties. PURPOSE: The aim of this study was to determine the effect of polymerization under pressure on the indirect tensile mechanical properties (stiffness and diametral tensile strength) of several light-polymerized composites. MATERIAL AND METHODS: Five light-polymerized composites were tested: Brilliant, Z100, TPH Spectrum, Prodigy, and Pertac Hybrid. A total of 80 cylindrical disk specimens (6 mm x 2 mm) were prepared for each material in a special mold that enabled polymerization under pressure (PUP). An equal number of specimens were polymerized under surface pressures of 0,.35,.71 and 1.06 MPa (n = 20). Stiffness (N/mm) and diametral tensile strength (DTS) (MPa) were analyzed while loading the specimen to failure with a loading machine. Two-way analysis of variance and Weibull analyses were applied (alpha=5%). RESULTS: Material type had a statistically significant influence on both DTS and stiffness (P<.0001). Differences up to 33% in DTS and up to 70% in stiffness values were found among the tested materials. Loading (PUP) had a significant influence on stiffness (P<.03) and DTS (P<.0001). PUP caused an increase in DTS values for Brilliant, Z100, and Prodigy of about 20% (P<.001) and increased stiffness only for Brilliant (15%). However, the amount of pressure needed for the improvement was different between materials (interaction between materials and loadings) (P<.0005). Weibull statistics showed that PUP improved the chances for reducing flaws in a material. CONCLUSION: Polymerizing material under pressure can improve its DTS and stiffness. However, the pressure needed for the procedure is material dependent.

Analysis of Variance↗
PubMed2003

Reduction of polymerization shrinkage stress and marginal microleakage using soft-start polymerization.

PURPOSE: This study evaluated the influence of a soft-start light-curing exposure on polymerization shrinkage stress and marginal integrity of adhesive restorations. MATERIALS AND METHODS: Six resin-based composites (Pertac II, Tetric Ceram, Definite, Surefil, Solitaire, and Visio-Molar) were adhesively bonded to a cylindrical cavity (n = 9 per material/light) in a photoelastic material. Visible light-curing was applied using either the standard polymerization mode (800 mW/cm2 exposure duration 40 s) of the curing light (Elipar TriLight, 3M ESPE) or the exponential mode from the same device (ramp-curing: 150 mW/cm2 to 800 mW/cm2 within the first 15 s of a total curing time of 40 s). Polymerization stress was calculated at 5 minutes, 1 hour, and 24 hours postexposure from the second-order isochromatic curves obtained from photoelastic images (Matrox-Inspector). Two standardized Class V preparations were made each on the facial and lingual surfaces of 80 extracted human molars and premolars. Resin restorative systems (Pertac II/EBS Multi, Tetric Ceram/Syntac, Definite/Etch&Prime 3.0, and Surefil/Prime & Bond 2.1) were exposed using both light exposure modes (n = 20). Marginal dye penetration (2% methylene blue) was investigated separately for enamel and cementum margins after thermocycling. To obtain information on equivalent depth of cure, relative surface hardness measurements were performed on resin samples of the same material at the top surface and at 1.5 mm and 3.0 mm thickness (Zwick 3212, 10 N). RESULTS: A significant (p < .01) reduction in polymerization stress of 7.1% for Pertac II, 4.1% for Tetric Ceram, 3.6% for Definite, 3.7% for Surefil, and 6.2% for Solitaire was observed when using the exponential mode as opposed to the standard. A significant (p = .04) reduction of marginal dye penetration was found only for Pertac II/EBS Multi at the cementum margins when the soft-start polymerization was used. For the sample thickness of 3 mm, a significant higher relative bottom to top surface ratio in favor of the standard exposure mode was found (p = .001). CLINICAL SIGNIFICANCE: Depending on the restorative material, soft-start polymerization may lead to a significant reduction in marginal microleakage of adhesive Class V restorations. This effect might be attributable to a significantly lower polymerization stress, as seen from photoelastic analysis, and/or a decrease in the degree of conversion, as deducted from surface hardness ratios. However, the effect of soft-start curing mode depends on the material itself, with the most effective response from hybrid resin-based composites.

Acetone↗
PubMed1980

The effects of cytochalasins on actin polymerization and actin ATPase provide insights into the mechanism of polymerization.

Substoichiometric concentrations of cytochalasin D inhibited the rate of polymerization of actin in 0.5 mM MgCl2, increased its critical concentration and lowered its steady state viscosity. Stoichiometric concentrations of cytochalasin D in 0.5 mM MgCl2 and even substoichiometric concentrations of cytochalasin D in 30 mM KCl, however, accelerated the rate of actin polymerization, although still lowering the final steady state viscosity. Cytochalasin B, at all concentrations in 0.5 mM MgCl2 or in 30 mM KCl, accelerated the rate of polymerization and lowered the final steady state viscosity. In 0.5 mM MgCl2, cytochalasin D uncoupled the actin ATPase activity from actin polymerization, increasing the ATPase rate by at least 20 times while inhibiting polymerization. Cytochalasin B had a very much lower stimulating effect. Neither cytochalasin D nor B affected the actin ATPase activity in 30 mM KCl. The properties of cytochalasin E were intermediate between those of cytochalasin D and B. Cytochalasin D also stimulated the ATPase activity of monomeric actin in the absence of MgCl2 and KCl and, to a much greater extent, stimulated the ATPase activity of monomeric actin below its critical concentration in 0.5 mM MgCl2. Both above and below its critical concentration and in the presence and absence of cytochalasin D, the initial rate of actin ATPase activity, when little or no polymerization had occurred, was directly proportional to the actin concentration and, therefore, apparently was independent of actin-actin interactions. To rationalize all these data, a working model has been proposed in which the first step of actin polymerization is the conversion of monomeric actin-bound ATP, A . ATP, to monomeric actin-bound ADP and Pi, A* . ADP . Pi, which, like the preferred growing end of an actin filament, can bind cytochalasins.

Actins↗
PubMed2001

Mechanistic Rationale of a Palladium-Catalyzed Allylic Substitution Polymerization-Carbon-Carbon Bond-Forming Polycondensation out of Stoichiometric Control by Cascade Bidirectional Allylation This work was supported by a Grant-in-Aid for Scientific Research (No. 12750778) from the Ministry of Education, Science, Sports, and Culture, Japan. A fellowship to K.T. from the Japan Society for the Promotion of Science for Young Scientists is gratefully acknowledged. In this contribution, the term "out of stoichiometric control" means that when reagent 2 a is used in excess, the polymerization is under stoichiometric control, whereas when 1 is in excess, the polymerization is not under stoichiometric control.

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Journal Article↗
PubMed1992

Polymeric porogens used in the preparation of novel monodispersed macroporous polymeric separation media for high-performance liquid chromatography.

A novel approach to monosized macroporous polymeric separation media with vastly enhanced pore size distributions and chromatographic properties has been developed. Key to this approach is the combined use of monodispersed polymeric particles and suitable solvents as porogens in the copolymerization of styrene and divinylbenzene. Following polymerization, the polymeric porogen is dissolved, leaving behind the monosized beads with a controlled pore structure. The exact pore size and pore size distribution of the final beads are largely controlled by the amount of soluble polymer in the polymerizing mixture: the larger the proportion of soluble polymer in the system, the larger the pores. The uniformly sized macroporous beads prepared with an optimized ratio of polymeric and low molecular weight porogens proved to be very efficient even in short columns for the separation of polystyrene standards in the SEC mode and the separation of proteins in the reversed-phase mode. The relationship between pore size and specific surface area, on one hand, and chromatographic properties of the stationary phase, on the other, have been clearly documented.

Chromatography, High Pressure Liquid↗
PubMed2003

Molecular cloning of a chondroitin polymerizing factor that cooperates with chondroitin synthase for chondroitin polymerization.

We recently cloned human chondroitin synthase (ChSy) exhibiting the glucuronyltransferase-II (GlcATII) and N-acetylgalactosaminyltransferase-II (GalNAcTII) activities responsible for the biosynthesis of repeating disaccharide units of chondroitin sulfate, but chondroitin polymerization was not demonstrated in vitro using the recombinant ChSy. We report here that the chondroitin polymerizing activity requires concomitant expression of a novel protein designated chondroitin polymerizing factor (ChPF) with ChSy. The human ChPF consists of 775 amino acids with a type II transmembrane protein topology. The amino acid sequence displayed 23% identity to that of human ChSy. The expression of a soluble recombinant form of the protein in COS-1 cells produced a protein with little GlcAT-II or GalNAcT-II activity. In contrast, coexpression of the ChPF and ChSy yielded markedly augmented glycosyltransferase activities, whereas simple mixing of the two separately expressed proteins did not. Moreover, using both UDP-glucuronic acid (GlcUA) and UDP-N-acetylgalactosamine (GalNAc) as sugar donors, chondroitin polymerization was demonstrated on the so-called glycosaminoglycan-protein linkage region tetrasaccharide sequence of alpha-thrombomodulin. These results suggested that the ChPF acts as a specific activating factor for ChSy in chondroitin polymerization. The coding region of the ChPF was divided into four discrete exons and localized to chromosome 2q35-q36. Northern blot analysis revealed that the ChPF gene exhibited a markedly different expression pattern among various human tissues, which was similar to that of ChSy. Thus, the ChPF is required for chondroitin polymerizing activity of mammalian ChSy.

Amino Acid Sequence↗
PubMed2005

Properties of an indirect composite material polymerized with two different laboratory polymerizing systems.

The purpose of the current study was to evaluate the performance of two laboratory light polymerization systems used to polymerize an indirect composite (Sinfony). A two-step polymerization system (Visio-Alfa and Beta) and a halogen-metal halide unit (Twinkle MIII) were assessed. The composite was polymerized either with the Visio units or with the MIII unit for different exposure periods. Knoop hardness, water sorption, and solubility in water of the composite polymerized with the following modes were determined: Visio, 15 minutes; MIII, 30, 60, 90, 120, and 180 seconds. Extension of light exposure time to the MIII unit improved the hardness of the composite from 30.5 (30 s) to 40.7 (180 s), whereas hardness obtained with the Visio units resulted in 24.8 (15 minutes). Water sorption and solubility of the composite were greater when it was polymerized with the Visio units than with the MIII unit.

Absorption↗
PubMed1976

Polymerization of Acanthamoeba actin. Kinetics, thermodynamics, and co-polymerization with muscle actin.

The kinetics and thermodynamics for the polymerization of purified Acanthamoeba actin were studied and compared to muscle actin. Polymerization was qualitatively similar for the two actins with a rate-limiting nucleation step followed by rapid polymer extension. Polymerization occurred only above a threshold critical concentration which varied with polymerization conditions for each actin. In the presence of 2 mM MgCl2, nucleation of both actins was rapid and their critical concentrations were similarly low and not detectably dependent on temperature. In 0.1 M KCl, the rates of nucleation of both actins were much slower than when Mg2+ was present and were significantly different from each other. Also, under these conditions, the critical concentrations of Acanthamoeba and muscle actin were significantly different and both varied markedly with temperature. These quantitative differences between the two actins could be attributed to differences in both their enthalpies and entropies of polymerization, Acanthamoeba actin having the more positive deltaH and delta S. Co-polymerization of the two actins was also demonstrated. Overall, however, there were no qualitative differences between Acanthamoeba and muscle actin that would suggest a unique role for the monomer-polymer equilibrium of cytoplasmic actin in cell motility.

Actins↗
PubMed1984

Polymerization of AS hybrid hemoglobin. Potent inhibitory effect of hemoglobin A on the polymerization of AS hybrid hemoglobin.

Asymmetrically cross-linked AS hybrid hemoglobin (Hb AS-fumarate) was prepared by reacting a mixture of oxy-Hb A and oxy-Hb S with a cross-linking agent, bis(3,5-dibromosalicyl)fumarate. Kinetics of the polymerization of Hb AS-fumarate in 1.8 M phosphate buffer showed that Hb AS-fumarate polymerized similarly to Hb S-fumarate despite the presence of a beta A chain. The kinetics of the polymerization of a mixture of Hb AS-fumarate and Hb S-fumarate was similar to that of Hb S-fumarate or Hb AS-fumarate alone. However, when Hb AS-fumarate was mixed with Hb A, the delay time prior to polymerization of the mixture was markedly prolonged. Although the solubility of Hb AS-fumarate was similar to that of Hb S-fumarate, it nearly doubled upon the addition of Hb A. Analysis of Hb A in the polymer phase showed that a significant amount (35-40%) of Hb A copolymerized with Hb AS-fumarate. No such effect was observed when Hb A was mixed with Hb S-fumarate, where the delay time prior to polymerization and the solubility of the mixture were regulated by the concentration of Hb S-fumarate in the mixture. The strong inhibitory effect of Hb A on the polymerization of Hb AS hybrid hemoglobin may help explain the benign clinical course in sickle cell trait.

Chromatography, High Pressure Liquid↗
PubMed2004

Calcium-binding site beta 2, adjacent to the "b" polymerization site, modulates lateral aggregation of protofibrils during fibrin polymerization.

Structural analysis of recombinant fibrinogen fragment D revealed that the calcium-binding site (beta2-site) composed of residues BbetaAsp261, BbetaAsp398, BbetaGly263, and gammaGlu132 is modulated by the "B:b" interaction. To determine the beta2-site's role in polymerization, we engineered variant fibrinogen gammaE132A in which calcium binding to the beta2-site was disrupted by replacing glutamic acid at gamma132 with alanine. We compared polymerization of gammaE132A to normal fibrinogen as a function of calcium concentration. Polymerization of gammaE132A at concentrations of calcium <or=1 mM exhibited an uncharacteristic 2-3-fold increase in lateral aggregation and fiber thickness compared to normal fibrinogen, while polymerization of variant and normal were indistinguishable at 10 mM calcium. These results suggest that the beta2-site controls the extent of lateral aggregation. That is, when the calcium anchor (beta2-site) is eliminated before "B:b" interactions occur then lateral aggregation is enhanced. We solved structures of fragment D of gammaE132A fibrinogen (rfD-gammaE132A) with and without Gly-His-Arg-Pro-amide (GHRPam) and found no change to the global structure. X-ray diffraction data showed GHRPam binding in the "a" and "b" polymerization sites and that calcium could still bind to the beta2-site of gammaE132A fibrinogen at 70 mM calcium. We found that the gamma2 calcium-binding site (in loop gamma294-301) did not have calcium bound in the structure of fragment D of gammaE132A fibrinogen with GHRPam bound (rfD-gammaE132A+GH). Analysis of structures rfD-gammaE132A+GH and rfD-BbetaD398A+GH indicated that differences in calcium occupation of the gamma2-site resulted from minor conformational changes provoked by crystal packing and GHRPam binding to the "a" site did not directly modulate calcium binding to this site.

Alanine↗
PubMed1998

Radical Nature of Cu-Catalyzed Controlled Radical Polymerizations (Atom Transfer Radical Polymerization).

Copper-catalyzed atom transfer radical polymerization (ATRP) is one of the most robust and precise techniques for controlling radical polymerization. The very good control of molecular weights, polydispersities, functionalities, chain composition, and topologies unusual for radical systems combined with the application of transition metals as catalysts requires more detailed mechanistic studies and proof of the radical nature of active species. The following results are in agreement with the radical nature of ATRP: reverse ATRP, chemoselectivities similar to those for conventional radical polymerization (effect of additives and inhibitors/scavengers, reactivity ratios, transfer coefficients), regioselectivities similar to those for conventional radical polymerization (low proportion of head-to-head units and expected structure of both tail and head end groups), stereoselectivities (tacticities) similar to that in conventional radical polymerization, EPR detection of X-Mtn+1 species resulting from the persistent radical effect, and confirmation of the termination by doubling molecular weights as well as cross-linking with multifunctional initiators and inimers. In addition, it seems that, in most ATRP systems, the contribution of degenerative transfer and reversible formation of organometallic intermediates is small and a halogen atom is transferred in the concerted process rather than in a two-step process with the involvement of radical anions.

Journal Article↗
PubMed1986

An intermediate state of G-actin between native and denatured: polymerization rate decreases but extent of polymerization remains unchanged.

The rate of actin polymerization gradually decreased without changing the final level of polymerization, when incubated in the presence of 0.2 mM ATP at pH 8.0 and 25 degrees C. This change was much faster in Mg2+-actin than Ca2+-actin, and Mg2+-actin became denatured and unpolymerizable on prolonged incubation. The drop in the polymerization rate was due both to weakened nucleation and a slowed elongation rate in the incubated actin. The change in the polymerization rate was partially reversible by storing the sample at 0 degrees C. When the rate of polymerization dropped markedly on prolonged incubation, a gel filtration profile showed that Ca2+-actin existed as monomer not as oligomer. On the other hand, Mg2+-actin formed dimers, and other oligomers, as revealed by crosslinking analysis. There were changes in fluorescence intensities due to tyrosine and/or tryptophan residues of the actin molecule, and in difference absorption spectra, suggesting that conformational changes intermediate between native and denatured states occurred during incubation.

Actins↗
PubMed2004

Polymerized alpha-antitrypsin is present on lung vascular endothelium. New insights into the biological significance of alpha-antitrypsin polymerization.

AIMS: The damage to lung tissue in chronic obstructive pulmonary disease (COPD) may involve the progressive loss of pulmonary vascular endothelial cells. Endothelial binding of alpha1-antitrypsin (alpha1-AT) derived from plasma has been identified, and alpha1-AT deficiency is a known genetic risk factor associated with alpha1-AT polymerization and COPD development. Therefore, in the present study we aimed to investigate if alpha1-AT is present on the lung vascular endothelium, and if it is in a polymeric form. METHODS AND RESULTS: Postmortem paraffin-embedded tissue specimens from 15 COPD (chronic bronchitis and emphysema) cases with and without Z alpha1-AT (Glu342Lys) deficiency and from 10 cases without signs of COPD were studied. Immunohistochemistry was performed using the streptavidin-biotin method with a monoclonal ATZ11 antibody specific for polymeric alpha1-AT, and polyclonal antibodies against human alpha1-AT and neutrophil elastase. Vascular endothelium showed intense staining for alpha1-AT with the ATZ11 antibody in all cases; however, intensity of staining in patients with alpha1-AT deficiency was greater. No endothelial staining was observed with the anti-elastase antibody. CONCLUSIONS: This is the first demonstration that alpha1-AT bound to the vascular endothelium of lungs is in a polymeric form, which also suggests a possible previously unknown role for polymeric alpha1-AT in vivo.

Endothelium, Vascular↗
PubMed2001

Fibrinogen Matsumoto V: a variant with Aalpha19 Arg-->Gly (AGG-->GGG). Comparison between fibrin polymerization stimulated by thrombin or reptilase and fibrin monomer polymerization.

Fibrinogen Matsumoto V (M-V) is a dysfibrinogen identified in a 52-year-old woman with systemic lupus erythematous. The triplet AGG encoding the amino acid residue Aalpha19 was replaced by GGG, resulting in the substitution of Arg-->Gly. Residue Aalpha19 has been shown to be one of the most important amino acids in the so-called 'A' site or alpha-chain knob. The thrombin-catalyzed release of fibrinopeptide A from M-V fibrinogen was only slightly delayed yet release of fibrinopeptide B was significantly delayed. Both thrombin-catalyzed fibrin polymerization and fibrin monomer polymerization were markedly impaired compared to normal fibrinogen. In addition, reptilase-catalyzed fibrin polymerization of M-V was much more impaired than thrombin-catalyzed fibrin polymerization. These results indicate 'B' and/or 'b' site of M-V fibrinogen play a more important role in thrombin-catalyzed fibrin polymerization than that of normal control fibrinogen.

Batroxobin↗
PubMed2002

The carboxyl-terminal domains of IgA and IgM direct isotype-specific polymerization and interaction with the polymeric immunoglobulin receptor.

Mucosal surfaces are protected by polymeric immunoglobulins that are transported across the epithelium by the polymeric immunoglobulin receptor (pIgR). Only polymeric IgA and IgM containing a small polypeptide called the "joining" (J) chain can bind to the pIgR. J chain-positive IgA consists of dimers, and some larger polymers, whereas only IgM pentamers incorporate the J chain. We made domain swap chimeras between human IgA1 and IgM and found that the COOH-terminal domains of the heavy chains (Calpha3 and Cmu4, respectively) dictated the size of the polymers formed and also which polymers incorporated the J chain. We also showed that chimeric IgM molecules engineered to contain Calpha3 were able to bind the rabbit pIgR. Since the rabbit pIgR normally does not bind IgM, these results suggest that the COOH-terminal domain of the polymeric immunoglobulins is primarily responsible for interaction with the pIgR. Finally, we made a novel chimeric IgA immunoglobulin, containing the terminal domain from IgM. This recombinant molecule formed J chain-containing pentamers that could, like IgA, efficiently form covalent complexes with the human pIgR ectodomain, known as secretory component.

Animals↗