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PubMedDate not supplied

Effect of chemical disinfectants and repair materials on the transverse strength of repaired heat-polymerized acrylic resin.

PURPOSE: The purpose of this study was to evaluate both the effects of immersion in different chemical disinfectant solutions and the type of repair material on the transverse strength of repaired heat-polymerized acrylic resin. MATERIALS AND METHODS: A total of 110 rectangular specimens (65 x 10 x 3 mm) of heat-polymerized acrylic resin (Triplex) were fabricated. After polymerization, the specimens were polished, then stored in distilled water at 37 degrees C for 1 week. The specimens were divided into 11 groups (n = 10) coded A to K. Specimens of Group A remained intact (control). The specimens of Groups C to F and Groups H to K were immersed in the following chemical disinfectant solutions (1%, 2.5%, and 5.25% sodium hypochlorite and 2% glutaraldehyde, respectively) for 10 minutes. The specimens of all groups except those of Group A were sectioned in the middle to create 10 mm gaps and repaired with the same resin (Groups B to F) and autopolymerizing acrylic resin (Groups G to K). The specimens of Groups C to F and Groups H to K were again immersed in the disinfectant solutions in the same sequence. The transverse strength (N/mm(2)) was tested for failure in a universal testing machine, at a crosshead speed of 5 mm/min. Two-way analysis of variance (ANOVA) was performed to evaluate the effects of both the disinfectant solutions and repair materials on the transverse strength of repaired specimens. All data were statistically analyzed using one-way analysis of variance followed by Tukey's test at 95% confidence level. RESULTS: The repaired specimens treated with/without disinfectant solutions showed similar (p > 0.05) transverse strength values. No differences (p > 0.05) were detected among the repaired specimens either with heat-polymerized or autopolymerizing acrylic resins. The intact specimens showed transverse strength values (86.9 +/- 11.8) significantly higher (p < 0.05) than the values of the repaired specimens. CONCLUSIONS: Among the repaired specimens, transverse strength was not affected after immersion in the disinfectants for the immersion period tested (10 min). The repair material, either heat-polymerized or autopolymerizing acrylic resin, had no effect on the transverse strength of the repaired acrylic resin specimens.

Acrylic Resins↗
PubMed2001

Topochemical polymerization of C70 controlled by monomer crystal packing.

Polymeric forms of C60 are now well known, but numerous attempts to obtain C70 in a polymeric state have yielded only dimers. Polymeric C70 has now been synthesized by treatment of hexagonally packed C70 single crystals under moderate hydrostatic pressure (2 gigapascals) at elevated temperature (300 degrees C), which confirms predictions from our modeling of polymeric structures of C70. Single-crystal x-ray diffraction shows that the molecules are bridged into polymeric zigzag chains that extend along the c axis of the parent structure. Solid-state nuclear magnetic resonance and Raman data provide evidence for covalent chemical bonding between the C70 cages.

Journal Article↗
PubMed1998

Bacterial SOS checkpoint protein SulA inhibits polymerization of purified FtsZ cell division protein.

Cell division of Escherichia coli is inhibited when the SulA protein is induced in response to DNA damage as part of the SOS checkpoint control system. The SulA protein interacts with the tubulin-like FtsZ division protein. We investigated the effects of purified SulA upon FtsZ. SulA protein inhibits the polymerization and the GTPase activity of FtsZ, while point mutant SulA proteins show little effect on either of these FtsZ activities. SulA did not inhibit the polymerization of purified FtsZ2 mutant protein, which was originally isolated as insensitive to SulA. These studies define polymerization assays for FtsZ which respond to an authentic cellular regulator. The observations presented here support the notion that polymerization of FtsZ is central to its cellular role and that direct, reversible inhibition of FtsZ polymerization by SulA may account for division inhibition.

Bacterial Proteins↗
PubMedDate not supplied

Modulation of actin polymerization by an exogenous protein, lysozyme.

Several methods (fluorescence, high- and low-shear viscosity, and electron microscopy) have been applied to measure the effects of lysozyme on actin polymerization. Under our conditions, at pH 8.0 and 20 degrees C, lysozyme is predominantly dimeric and its major effect is to inhibit the steady-state polymerization of actin. Those actin filaments formed in the presence of lysozyme are significantly shortened with recurrent amorphous densities along the filament length. However, at pH 6.4 and 37 degrees C, lysozyme is monomeric and actin filament cross-linking is observed. We reasoned that in hen egg white lysozyme the tripeptide L-arginyl-glycyl-aspartate (RGD), a sequence capable of mimicking a portion of the receptor sites of extracellular matrix proteins, might be important in lysozyme self-association and, therefore, actin-lysozyme interaction. The presence of RGD in the lysozyme-actin polymerizing solutions at pH 8.0 and 20 degrees C caused an inhibition of the dimeric lysozyme effects, while RGD alone had no effects on actin polymerization. Therefore, RGD most likely binds to a complementary RGD sequence on lysozyme and alters its ability to interact with actin and modify polymerization.

Actin Cytoskeleton↗
PubMed1996

EJ-Ras inhibits phospholipase C gamma 1 but not actin polymerization induced by platelet-derived growth factor-BB via phosphatidylinositol 3-kinase.

Transformation of fibroblast-like cells (NIH 3T3) by a constitutively activated GTP-bound isoform of p21ras (EJ-Ras) produces morphogenic changes characterized by decreased attachment to the substratum, with retraction and rounding of the cell body. Transformed fibroblasts lose their "stressed" conformation and adopt a "relaxed" morphology. The specific molecular mechanisms responsible for these changes remain uncharacterized. We found that EJ-Ras transformation of NIH 3T3 cells decreased the cellular content of polymerized actin, particularly at the expense of actin stress fibers, but induced the accumulation of actin filaments in peripheral ruffling membranes. Polymerization of actin could be induced in EJ-Ras-transformed cells by exposure to platelet-derived growth factor (PDGF)-BB to an extent similar to that observed in wild-type NIH 3T3 cells. In EJ-Ras cells, actin polymerization was independent of phospholipase C gamma 1 (PLC gamma 1) activity, because inositol tris-phosphate (IP3) production observed in control NIH 3T3 cells in response to PDGF-BB was absent. Although PDGF-BB did stimulate tyrosine phosphorylation of PLC gamma 1, the phospholipase was strongly inhibited by an inhibitory factor present in the cytoplasm of EJ-Ras-transformed cells. In addition, cytoplasmic extracts of EJ-Ras, but not of control cells, inhibited phosphatidylinositol 4,5-diphosphate (PIP2) hydrolysis catalyzed by a recombinant PLC gamma 1 in vitro. Although PIP2 hydrolysis could not contribute to the reorganization of the actin cytoskeleton induced by PDGF-BB in EJ-Ras-transformed cells, phosphatidylinositol 3-kinase (PI3-K) was necessary for actin polymerization. Wortmannin, a specific PI3-K inhibitor, not only blocked actin polymerization in both control and EJ-Ras-transformed cells but actually led to rapid actin depolymerization when these cells were exposed to PDGF-BB. Thus, in EJ-Ras-transformed cells, cell morphogenic changes in response to PDGF-BB rely importantly on PI3-K and can occur in the complete absence of IP3 production despite tyrosine phosphorylation of PLC gamma 1.

3T3 Cells↗
PubMed2000

Surface characterization and platelet adhesion studies on fluorocarbons prepared by plasma-induced graft polymerization.

It is believed that the interactions between the biological environment and biomaterial surface are the key factors influencing its biocompatibility. Therefore, plasma processing, which can vary the surface properties without altering the bulk properties, has been considered as one of the important techniques for improving a materials' biocompatibility. In this investigation, plasma-induced grafting polymerization of vinylidene fluoride (VDF) and chlorotrifluoroethylene (CTFE), instead of direct plasma polymerization, was attempted with an aim to improve the substrate blood compatibility. Contact angle measurement indicated both fluorocarbon-grafted Pdyethylenes (PEs) are hydrophobic. Due to the additional fluorine and chlorine atoms on the CTFE chain, the PCTFE-grafted PE exhibited a higher hydrophobicity than the PVDF-grafted one. ESCA analysis has revealed that these two plasma-induced fluorocarbon deposits contain almost no CFx (x > 2) binding on the surface layer, indicating the grafting polymerization mainly follows the free radical mechanism instead of the molecule-highly-fragmented reaction steps commonly seen in the direct plasma polymerization treatment. In addition, ATR-FTIR has shown the surface chemical configuration of these PVDF- and PCTFE-grafted PEs to be very similar to those of the bulk samples of PVDF and PCTFE. The surface roughness decreased after oxygen plasma treatment and was further reduced by VDF and CTFE grafting polymerization. In vitro platelet adhesion testing indicated these two fluorocarbon grafted PEs are less platelet-activating than the nontreated PE control and oxygen plasma activated one.

Biocompatible Materials↗
PubMed2006

Synthesis of SiO2-coated Bi2S3/poly(styrene) nanocomposites by in-situ polymerization.

New nanocomposites containing silica-coated Bi2S3 nanofibers were synthesised by in situ polymerization using two distinct synthetic strategies: emulsion and suspension polymerization. Transmission and scanning electron microscopy of the nanocomposite particles showed that in both cases the Bi2S3/SiO2 nanoparticles were densely coated with poly(styrene). In situ emulsion polymerization afforded nanocomposites in which the nanofibers were coated with polymer spheres whilst suspension polymerization gives rise to a homogeneous polymer layer coat. The morphology of the poly(styrene) coating observed is discussed considering the surface modification of the nanofibers and the polymerization technique involved.

Bismuth↗
PubMed1979

Quantitative assessment of polymerized and depolymerized platelet microtubules. Changes caused by aggregating agents.

The equilibrium between assembled and disassembled microtubules was studied in human platelets exposed to aggregating agents. Soluble and insoluble tubulin were "frozen" by addition of a glycerol-dimethyl sulfoxide-containing medium. The two pools were estimated by measuring the colchicine binding activities of total and polymerized tubulin. Resting platelets were found to contain an average of 56.2 mug tubulin/1 x 10(9) cells of which 56.7% was in polymerized form. Platelet aggregation induced by thrombin, ADP, epinephrine, or collagen produced a transient decrease in the pool of polymerized tubulin which was evident within 15 s after addition of the aggregating agent. A return to base-line values occurred within 1-4 min depending upon the specific aggregating agent used. Neither secretory release nor aggregation of platelets were found to be prerequisites for the temporary disturbance of the equilibrium between soluble and polymerized tubulin. With thrombin as the aggregating agent a clear threshold concentration could be demonstrated above with a dose-dependent dissociation response of microtubules was evident. We conclude that microtubules exist in a dynamic equilibrium between polymerized and depolymerized forms in human platelets, which is transiently disturbed by their interaction with aggregating agents.

Blood Platelets↗
PubMed1983

"Fibrinogen Tokyo II". An abnormal fibrinogen with an impaired polymerization site on the aligned DD domain of fibrin molecules.

A hereditary dysfibrinogenemia associated with defective aggregation of fibrin monomers was found in a 39-yr-old female and in the members of her immediate family, who had all been asymptomatic. The abnormality was probably due to an impaired polymerization site exposed in the DD domain of two adjacent fibrin molecules, because plasmic fragment DD derived from the propositus' cross-linked fibrin bound far less tightly to insolubilized normal fragment E than that from the normal one. Its complementary polymerization site in the E domain of fibrin, which was exposed by thrombin cleavage, and the polymerization site in the D domain of fibrinogen, which was available without activation by thrombin, were both found to be normal. More anodal migration of the abnormal fragment DD than the normal one, as shown by immunoelectrophoresis, seemed to support our concept that the mutation most likely resides in the D domain of the abnormal fibrinogen molecule at or near a region closely related to the polymerization site that is exposed when two fibrin molecules are linearly aligned. The work of others on the polymerization of normal fibrin with different techniques yielded results consistent with our conclusions. We tentatively designate this type of abnormal fibrinogen "fibrinogen Tokyo II," but its possible identity with other abnormalities of fibrinogen reported heretofore is not excluded.

Adult↗
PubMed1999

The effects of light intensity, temperature, and comonomer composition on the polymerization behavior of dimethacrylate dental resins.

One of the most common combinations for the organic phase of dental restorative materials is BisGMA (2,2bis[4-(2-hydroxy-3-methacryloyloxypropoxy) phenyl]propane) and TEGDMA (triethylene glycol dimethacrylate). However, this copolymer has some drawbacks, such as volume shrinkage during cure and lack of complete double-bond conversion. If the properties of this system are to be improved, an attempt must be made to understand the underlying kinetics of the reaction. This work examines the effects of light intensity, temperature, and composition on the polymerization behavior of BisGMA/TEGDMA copolymerizations. Using differential scanning calorimetry, we monitored the rates of photopolymerization for various experimental conditions. The BisGMA/TEGDMA copolymerization behaved similarly to other dimethacrylate systems and exhibited diffusion-controlled kinetics. It was found that the maximum rate of polymerization was significantly affected by the intensity of the light, and the temperature of the polymerization affected the conversion at which the maximum rate occurred. When the composition of the mixture was varied, it was discovered that the viscosity of the system played a significant role in the polymerization rate and the onset of reaction-diffusion-controlled termination. Mixtures which contained from 50 wt% to 75 wt% BisGMA displayed the highest maximum rate. This feature suggests that TEGDMA is an excellent diluent, since it increases the mobility of the reacting medium; however, the high reactivity is due to the presence of BisGMA. Therefore, based on compositional dependence, we conclude that the BisGMA portion of the mixture largely controls the polymerization mechanisms and kinetics.

Algorithms↗
PubMed1998

Release of drugs from polymeric hydrogels.

Hydrogels were prepared from 2-hydroxyethyl methacrylate and ethylene glycol dimethacrylate as cross-linking agent. Two different polymerization techniques were followed, namely bulk polymerization initiated by dibenzoyl peroxide and solution polymerization, in water, using a redox initiator system. Differences in the water desorption from swollen samples between the two types of the above products were recorded and attributed to the fact that those hydrogels were obtained in glassy or rubbery state, according to the polymerization technique. Also, the delivery of salicylic acid from samples of the above types was studied, and a faster release with higher ultimate delivery was displayed by the solution polymerization hydrogels.

Drug Carriers↗
PubMed2000

Mechanochemical solid-state polymerization (X): the influence of copolymer structure in copolymeric prodrugs on the nature of drug release.

From the standpoint of the mechanism of mechanochemical polymerization, two kinds of copolymeric prodrug, whose monomer sequence distribution (MSD) is different from each other, can be prepared by this polymerization under appropriate operational conditions: one is a random copolymer abundant in the longer block consisting of the same repeating units (multi-block copolymer), and the other is a block copolymer. To confirm the difference of MSD, the 13C-NMR spectra of poly(acrylamide-co-sodium acrylate) prepared by mechanochemical polymerization were measured and compared with the spectrum of that synthesized by a conventional radical-initiated solution polymerization, which produces the random copolymer normally. The results show that MSD in copolymers depends on the polymerization method (operational condition). We prepared three kinds of copolymeric prodrug consisting of acrylamide and vinyl monomer of 5-fluorouracil, whose MSD is different from one another. These copolymeric prodrugs had almost the same number average molecular weight, particle diameter and composition, and differed only in MSD. We compared the rate of drug release of these copolymeric prodrugs. The rate of drug release was the highest with the random copolymer, followed by the mechanochemically produced multi-block copolymer and the block copolymer. This result suggests that the rate of drug release depends on MSD of copolymeric prodrugs. These results are useful as they give a fundamental insight into the synthesis of copolymeric prodrugs having the desired rate of drug release.

Antimetabolites↗
PubMed2004

Z alpha1-antitrypsin polymerizes in the lung and acts as a neutrophil chemoattractant.

BACKGROUND: Alpha1-antitrypsin (A1AT) is an abundant protein that is synthesized in the liver and is secreted into the plasma. From the plasma, A1AT diffuses into various body compartments, including the lung where it provides much of the antiprotease protection. The current understanding of the pathogenesis of emphysema in A1AT-deficient individuals focuses on the polymerization of mutant protein within the liver, which results in a deficiency of circulating A1AT and a protease-antiprotease imbalance in the lungs. METHODS AND RESULTS: In this study, we evaluated BAL fluid samples from five healthy volunteers, five individuals with ZA1AT deficiency, and an individual with the PiZZ phenotype who had received a liver transplant. We show that the lung itself is a source of A1AT. In addition, the Z protein formed in the lung polymerizes, and these polymers are detectable in lung epithelial lining fluid by enzyme-linked immunosorbent assay and Western blot analysis. Finally, we show that polymeric ZA1AT is a potent neutrophil chemoattractant that is similar to polymerized MA1AT. CONCLUSIONS: Our findings suggest that the polymerization of locally produced ZA1AT is a contributory factor to the lung inflammation experienced by those with A1AT deficiency and that standard antiprotease therapies may not address this problem.

Adult↗
PubMed2002

An alternative method to reduce polymerization shrinkage in direct posterior composite restorations.

BACKGROUND: Polymerization shrinkage is one of dental clinicians' main concerns when placing direct, posterior, resin-based composite restorations. Evolving improvements associated with resin-based composite materials, dental adhesives, filling techniques and light curing have improved their predictability, but shrinkage problems remain. METHODS: The authors propose restoring enamel and dentin as two different substrates and describe new techniques for placing direct, posterior, resin-based composite restorations. These techniques use flowable and microhybrid resin-based composites that are polymerized with a progressive curing technique to restore dentin, as well as a microhybrid composite polymerized with a pulse-curing technique to restore enamel. Combined with an oblique, successive cusp buildup method, these techniques can minimize polymerization shrinkage greatly. CONCLUSIONS: Selection and appropriate use of materials, better placement techniques and control polymerization shrinkage may result in more predictable and esthetic Class II resin-based composite restorations. CLINICAL IMPLICATIONS: By using the techniques discussed by the authors, clinicians can reduce enamel microcracks and substantially improve the adaptation of resin-based composite to deep dentin. As a consequence, marginal discoloration, recurrent caries and postoperative sensitivity can be reduced, and longevity of these restorations potentially can be improved.

Acid Etching, Dental↗
PubMed2006

Polymeric micelles for drug delivery.

Polymeric micelles have been the subject of many studies in the field of drug delivery for the past two decades. The interest has specifically been focused on the potential application of polymeric micelles in three major areas in drug delivery: drug solubilisation, controlled drug release and drug targeting. In this context, polymeric micelles consisting of poly(ethylene oxide)-b-poly(propylene oxide), poly(ethylene oxide)-b-poly(ester)s and poly(ethylene oxide)-b-poly(amino acid)s have shown a great promise and are in the front line of development for various applications. The purpose of this manuscript is to provide an update on the current status of polymeric micelles for each application and highlight important parameters that may lead to the development of successful polymeric micellar systems for individual delivery requirements.

Animals↗
PubMed1982

Protein from macrophages inhibiting polymerization of actin.

The crude cytoplasmic extracts of macrophages showed a low actin-polymerization activity as compared with the purified actin preparations. This suggested that an actin-polymerization inhibitor should exist in the crude cytoplasmic extracts of macrophages. Thus, the isolation of actin-polymerization inhibiting protein from the crude extract was attempted. The protein with a high actin-polymerization inhibiting activity had a molecular weight of 65,000 daltons as determined by polyacrylamide gel electrophoresis in dodecyl sulfate, a Stokes radius of 33.8 A as measured by gel filtration and a sedimentation coefficient of 4.9 S as determined by analytical centrifugation. The actin-polymerization inhibiting activity was much higher in 0.1 M KCl than in 0.6 M KCl. It was not affected by either the presence or the absence of free Ca2+. It was considered that the protein is responsible for the large proportion of unpolymerized actin in the crude extract of macrophages.

Actins↗
PubMed2006

Promotion of optimized protein therapy by bioconjugation as a polymeric DDS.

In recent years, clinical applications of recombinantly produced bioactive proteins such as cytokines have attracted attention. However, since these recombinant proteins are rather unstable in vivo, their clinical use as therapeutic agents requires frequent administration at a high dosage. This regimen disrupts homeostasis and results in severe side effects. To overcome these problems, bioactive proteins have been conjugated with water-soluble synthetic (WSS) polymeric carriers. Chemical modification of a protein with a WSS polymeric carrier (bioconjugation) regulates tissue distribution, resulting in a selective increase in its desirable therapeutic effects and a decrease in undesirable side effects. Among several drug delivery system (DDS) technologies, bioconjugation has been recognized as one of the most efficient methods for improving therapeutic potency of proteins. However, for further enhancement of the therapeutic potency and safety of conjugated bioactive proteins, more precise regulation of the in vivo behavior of each protein is necessary for selective expression of its therapeutic effect. Therefore, alternative WSS polymeric modifiers in which new functions such as targeting and controlled release of drugs can be added are required for further development of bioconjugated drugs. Recently, we have synthesized a novel polymeric drug carrier, poly(vinylpyrrolidone-co-dimethyl maleic anhydride) [PVD], which was a powerful candidate drug carrier for cancer therapy. In this review, we introduce useful information that enabled us to design polymeric drug carriers and their application for protein therapy.

Antineoplastic Agents↗
PubMedDate not supplied

Comparisons of polymeric and conventional coagulants in arsenic(V) removal.

The removal of arsenic(V) from water was investigated under various coagulation conditions and compared to a variety of coagulation agents, including polymeric ferric chloride, polymeric ferric sulfate, polymeric aluminum chloride, polymeric aluminum sulfate, ferric chloride, ferric sulfate, aluminum chloride, and aluminum sulfate. Coagulation conditions evaluated include pH, temperature, type of coagulant, the addition of a coagulation aid, and initial arsenic(V) concentration. Results indicated that the arsenic removal efficiencies of polymeric coagulants were typically 10 to approximately 20% higher than those of their conventional coagulant counterparts.

Aluminum Compounds↗