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PubMed2004

Micropatterned composite membranes of polymerized and fluid lipid bilayers.

Micropatterned composite membranes of polymerized and fluid lipid bilayers were constructed on solid substrates. Lithographic photopolymerization of a diacetylene-containing phospholipid, 1,2-bis(10,12-tricosadiynoyl)-sn-glycero-3-phosphocholine (DiynePC), and subsequent removal of nonreacted monomers by a detergent solution (0.1 M sodium dodecyl sulfate (SDS)) yielded a patterned polymeric bilayer matrix on the substrate. Fluid lipid bilayers of phosphatidylcholine from egg yolk (egg-PC) were incorporated into the lipid-free wells surrounded by the polymeric bilayers through the process of fusion and reorganization of suspended small unilamellar vesicles. Spatial distribution of the fluid bilayers in the patterned bilayer depended on the degree of photopolymerization that in turn could be modulated by varying the applied UV irradiation dose. The polymeric bilayer domains blocked lateral diffusion of the fluid lipid bilayers and confined them in the defined areas (corrals), if the polymerization was conducted with a sufficiently large UV dose. On the other hand, lipid molecules of the fluid bilayers penetrated into the polymeric bilayer domains, if the UV dose was relatively small. A direct correlation was observed between the applied UV dose and the lateral diffusion coefficient of fluorescent marker molecules in the fluid bilayers embedded within the polymeric bilayer domains. Artificial control of lateral diffusion by polymeric bilayers may lead to the creation of complex and versatile biomimetic model membrane arrays.

Diffusion↗

PubMed2006

Conventional and high-intensity halogen light effects on polymerization shrinkage of orthodontic adhesives.

The objectives of this study were to compare the polymerization shrinkage of three orthodontic adhesives. In addition we wanted to determine the effectiveness of the high-intensity quartz tungsten halogen (HQTH) in curing orthodontic adhesives on polymerization shrinkage with that of the quartz tungsten halogen (QTH). A total of 120 glass ring molds were prepared using a low-speed saw. The internal surface of the glass rings were roughened and etched. Adhesive pastes were placed into the glass molds, which were sandwiched between two glass slides. Samples were divided into six groups according to the combination of three orthodontic adhesives (Kurasper F, Light Bond, and Transbond XT) and two light intensities. One half of each 40 samples of three adhesive pastes was polymerized for 20 seconds by a QTH (Hilux 350), and the other half was polymerized for 10 seconds by a HQTH (Optilux 501). The volumetric polymerization shrinkage for each system was measured through the specific density method modified by Puckett and Smith. Statistical analysis was performed using two-way analysis of variance for intergroup comparisons. The HQTH-curing unit resulted in a more polymerization shrinkage than did the QTH for all investigated adhesives. However, no statistically significant differences were found. The highest shrinkage was observed for Light Bond cured with HQTH (1.59 +/- 0.82%), and the lowest value was observed for Transbond XT cured with QTH (1.23 +/- 0.60%). There are no significant differences in polymerization shrinkage of the three investigated orthodontic adhesives when polymerized with a QTH or a HQTH.

Acid Etching, Dental↗

PubMed1998

Effect of polymerization temperature and time on the residual monomer content of denture base polymers.

The aim of this study was to investigate the effect of polymerization time and polymerization temperature on the residual methyl methacrylate (MMA) content of two heat-cured and two autopolymerized denture base polymers. Gas chromatography was used to determine the residual MMA content of three test specimens of each type of polymer. Increasing the polymerization temperature for the autopolymerized denture base resins from 30 degrees C to 60 degrees C decreased the residual MMA content of the polymer from an average of 4.6 wt% to 3.3 wt%. With the heat-cured denture base resins, a curing cycle at a polymerization temperature of 70 degrees C followed by a period at 100 degrees C significantly reduced the residual monomer content of the polymer when compared with a resin cured at 70 degrees C only. Polymerizing the heat-cured denture base resin at 100 degrees C only for various lengths of time significantly affected the residual MMA content of the polymer. The lowest residual MMA content (0.07 wt%) was obtained by polymerizing the heat-cured denture base resin at 100 degrees C for 12 h. The results of this study suggest that the polymerization temperature and polymerization time considerably affect the residual MMA content of denture base polymers.

Acrylic Resins↗

PubMed2005

Acceleration of yeast actin polymerization by yeast Arp2/3 complex does not require an Arp2/3-activating protein.

The Arp2/3 complex creates filament branches leading to an enhancement in the rate of actin polymerization. Work with Arp complexes from different sources indicated that it was inactive by itself, required an activating factor such as the Wiskott-Aldrich syndrome protein (WASP), and might exhibit a preference for ATP or ADP-P(i) actin. However, with yeast actin, P(i) release is almost concurrent with polymerization, eliminating the presence of an ADP-P(i) cap. We thus investigated the ability of the yeast Arp2/3 complex (yArp2/3) to facilitate yeast actin polymerization in the presence and absence of the Arp2/3-activating factor Las17p WA. yArp2/3 significantly accelerates yeast actin but not muscle actin polymerization in the absence of Las17p WA. The addition of Las17p WA further enhances yeast actin polymerization by yArp2/3 and allows the complex to now assist muscle actin polymerization. This actin isoform difference is not observed with bovine Arp2/3 complex, because the neural WASP VCA fragment is required for polymerization of both actins. Observation of individual branching filaments showed that Las17p WA increased the persistence of filament branches. Compared with wild type actin, the V159N mutant actin, proposed to be more ATP-like in behavior, exhibited an enhanced rate of polymerization in the presence of the yArp2/3 complex. yArp2/3 caused a significant rate of P(i) release prior to observation of an increase in filament mass but while branched structures were present. Thus, yeast F-actin can serve as a primary yArp2/3-activating factor, indicating that a newly formed yeast actin filament has a topology, unlike that of muscle actin, that is recognized specifically by yArp2/3.

Actin-Related Protein 2↗

PubMed2004

Hemoglobin polymerized with a naturally occurring crosslinking agent as a blood substitute: in vitro and in vivo studies.

A naturally occurring crosslinking agent, genipin, extracted from the fruits of Gardenia jasminoides ELLIS was used by our group to chemically modified biomolecules. Genipin and its related iridoid glucosides have been widely used as an antiphlogistic and cholagogue in herbal medicine. Our previous study showed that the cytotoxicity of genipin is significantly lower than glutaraldehyde. The study was to investigate the feasibility of using genipin to polymerize hemoglobin as a blood substitute. The results indicated that the rate of hemoglobin polymerization by glutaraldehyde was significantly faster than that by genipin and it readily produced polymers with molecular masses greater than 500,000 Da. It was found that the maximum degree of hemoglobin polymerization by genipin was approximately 40% if over-polymerization is to be prevented. With increasing the reaction temperature, hemoglobin concentration, and genipin-to-hemoglobin molar ratio, the duration taken to achieve the maximum degree of hemoglobin polymerization by genipin became significantly shorter. The P50 value of the unmodified hemoglobin was 9 mmHg, while that of the genipin-polymerized PLP-hemoglobin increased to 21 mmHg. It was found in a rat model that the genipin-polymerized PLP-hemoglobin resulted in a longer circulation time than the unmodified hemoglobin. In conclusion, the results of the study indicated that the genipin-polymerized hemoglobin solution has a lower oxygen affinity and a longer vascular retention time than the unmodified hemoglobin solution.

Animals↗

PubMed1988

Probing actin polymerization by intermolecular cross-linking.

We have used N,N'-1,4-phenylenebismaleimide, a bifunctional sulfhydryl cross-linking reagent, to probe the oligomeric state of actin during the early stages of its polymerization into filaments. We document that one of the first steps in the polymerization of globular monomeric actin (G-actin) under a wide variety of ionic conditions is the dimerization of a significant fraction of the G-actin monomer pool. As polymerization proceeds, the yield of this initial dimer ("lower" dimer with an apparent molecular mass of 86 kD by SDS-PAGE [LD]) is attenuated, while an actin filament dimer ("upper" dimer with an apparent molecular mass of 115 kD by SDS-PAGE [UD] as characterized [Elzinga, M., and J. J. Phelan. 1984. Proc. Natl. Acad. Sci. USA. 81:6599-6602]) is formed. This shift from LD to UD occurs concomitant with formation of filaments as assayed by N-(1-pyrenyl)iodoacetamide fluorescence enhancement and electron microscopy. Isolated cross-linked LD does not form filaments, while isolated cross-linked UD will assemble into filaments indistinguishable from those polymerized from unmodified G-actin under typical filament-forming conditions. The presence of cross-linked LD does not effect the kinetics of polymerization of actin monomer, whereas cross-linked UD shortens the "lag phase" of the polymerization reaction in a concentration-dependent fashion. Several converging lines of evidence suggest that, although accounting for a significant oligomeric species formed during early polymerization, the LD is incompatible with the helical symmetry defining the mature actin filament; however, it could represent the interfilament dimer found in paracrystalline arrays or filament bundles. Furthermore, the LD is compatible with the unit cell structure and symmetry common to various types of crystalline actin arrays (Aebi, U., W. E. Fowler, G. Isenberg, T. D. Pollard, and P. R. Smith. 1981. J. Cell Biol. 91:340-351) and might represent the major structural state in which a mutant beta-actin (Leavitt, J., G. Bushar, T. Kakunaga, H. Hamada, T. Hirakawa, D. Goldman, and C. Merril. 1982. Cell. 28:259-268) is arrested under polymerizing conditions.

Actin Cytoskeleton↗

PubMed1977

Physiological regulation of total tubulin and polymerized tubulin in tissues.

Polymerized and depolymerized forms of tubulin were measured in rat and mouse liver, rat islets, human lymphocytes, and platelets. The percent of the total tubulin present in the polymerized form varied from 30.3 +/- 1.5% in the liver of the fed rat to 89.2 +/- 0.2% in human platelets. Fasting decreased the total tubulin and to a greater extent the polymerized form of tubulin in both rat and mouse liver. Glucose feeding increased the polymerized tubulin without affecting the total tubulin content in rat liver. Phytohemagglutinin-stimulated lymphocytes exhibited at least a three-fold increase in total tubulin (expressed in terms of DNA content), which during the initial 48 h of incubation was accounted for in toto by an increase in polymerized tubulin. It is suggested that the lectin not only accelerates tubulin synthesis but also stimulated the polymerization process. Storage of platelets at 4 degrees C for 6 days resulted in a marked decrease in total tubulin and an even greater reduction in the polymerized form. It is concluded that both the total tubulin content and its degree of polymerization can be modulated independently by a wide variety of physiological factors.

Animals↗

PubMed1983

Kinetic analysis of actin polymerization.

The kinetics of actin polymerization were analyzed by measuring the changes in absorbance which accompany the G-F transformation of actin. In these studies, gel-filtered actin was polymerized in the absence of shearing stress under physiological ionic conditions. Self-polymerization was found to be characterized as a process having a lag phase followed by a pseudo-first-order decay process, suggesting that actin polymerization consists of distinct nucleation and elongation phases. The size of the nucleus was estimated to be two to four monomer units by analyzing the actin concentration-dependences of the rate constant for the pseudo-first-order process, the maximal rate of polymerization and the half-polymerization time. The elongation reaction was induced by mixing actin filament seeds with actin monomers under conditions where spontaneous nucleation is slow. This elongation was also found to be a pseudo-first-order process, indicating that spontaneous nucleation was negligible. Our data suggested that the initial rate of elongation was proportional to both the number concentration of actin filaments and the actin monomer concentration above the critical concentration, and that the depolymerization rate was proportional to the number concentration of actin filaments but independent of monomer concentration. The results of direct analysis of the depolymerization reaction were consistent with this suggestion. These studies strongly support the condensation polymerization mechanism as a model for actin polymerization.

Actins↗

PubMed1984

Action of a 19K protein from porcine brain on actin polymerization: a new functional class of actin-binding proteins.

A 19K protein isolated from porcine brain not only inhibits actin polymerization but depolymerizes actin filaments quickly. The protein reacts stoichiometrically with actin in a 1:1 molar ratio. When actin is induced to polymerize with salts in the presence of the brain 19K protein, the lag phase is prolonged, and the extent of polymerization is decreased, but the half-polymerization time is not increased. This can be explained by assuming that the 19K protein severs growing actin filaments and thus causes an increase in the number of filament ends during the polymerization process, thereby accelerating the overall polymerization. Moreover, the low-shear viscosity of actin filaments is reduced much more than the high-shear viscosity by the 19K protein, suggesting that actin filaments become shorter in the presence of the 19K protein than in its absence. Actin filament depolymerization by the 19K protein is much faster than that by brain profilin or than spontaneous depolymerization. This indicates that the 19K protein depolymerizes actin filaments not only by sequestering actin monomers but also by directly attacking the filaments. The number of actin filaments, measured by assaying the nucleating ability, is increased by substoichiometric concentrations of the 19K protein, irrespective of whether the protein is added to actin monomers before polymerization or added to performed actin filaments. These results suggest that the brain 19K protein not only stabilizes actin monomers but also cuts actin filaments, thereby decreasing the extent of actin polymerization and also changing the filament length. The action on actin of the actin-depolymerizing protein from starfish oocytes resembles that of the brain 19K protein, although the molecular weight of the starfish protein is slightly smaller. The brain 19K protein and starfish protein should be classified into a new functional group of actin-binding proteins.

Actin Depolymerizing Factors↗

PubMed2004

Effect of plasma arc curing on polymerization shrinkage of orthodontic adhesive resins.

The purpose of this study was to evaluate the polymerization shrinkage of three orthodontic adhesive resins when polymerized with a high-energy plasma arc light (1340 mW cm(-2)) and a conventional halogen light (500 mW cm(-2)), and to correlate the polymerization shrinkage with the degree of conversion. To equalize the total light energy delivered to the adhesive resin, irradiation time was varied between 3 or 6 s for a plasma arc-curing unit, and 8 or 16 s for a halogen light-curing unit. The polymerization shrinkage of adhesive resins during the light-curing process was measured using a computer-controlled mercury dilatometer and the degree of conversion was measured using Fourier transform infrared spectroscopy. A plasma arccuring unit produced significantly lower polymerization shrinkage than a halogen light-curing unit when the equivalent total light energy was irradiated to the orthodontic adhesive resins (P < 0.05). The magnitude of polymerization shrinkage was significantly different depending on the kind of adhesive resins (P < 0.05), but there was no significant correlation between the filler fraction and the polymerization shrinkage (r2 = 0.039). There was strong correlation (r2 = 0.787) between the polymerization shrinkage and the degree of conversion with a halogen light-curing unit, but poor correlation (r2 = 0.377) was observed with a plasma arc-curing unit.

Dental Bonding↗

PubMed2005

Effect of curing environment on mechanical properties and polymerizing behaviour of methyl-methacrylate autopolymerizing resin.

Methyl-methacrylate autopolymerizing resin is used for multiple applications. Therefore, the mechanical properties of autopolymerizing resin should be assessed comprehensively including strength, stiffness and hardness. Any methods that effectively improve these mechanical properties are desirable. The objective of this study is to examine the effects of the curing environment: air or water with/without pressure, and air or water temperature during polymerization, on the strength, stiffness and hardness of autopolymerizing resin. In addition, we examined the polymerizing behaviour associated with the mechanical properties. Autopolymerizing methyl-methacrylate resin (Unifast II) was polymerized under the following conditions: in air and water with/without pressure at 10, 23, 30, 40, 60 and 80 degrees C. The resin specimens were subjected to a transverse test (three-point flexural test) and micro-Brinell surface hardness test. Fractured surfaces of the specimens after the transverse test were examined using a scanning electron microscope (SEM). The transverse strength and transverse modulus increased with increasing curing temperature in both wet and dry conditions. Pressured wet conditions increased transverse strength and transverse modulus over non-pressured wet and dry conditions. The resin polymerized in dry conditions showed higher surface hardness than the one polymerized in wet conditions at matching temperature. The SEM images of fractured surfaces cured at lower temperature exhibited porosity within the polymer base and cracks between the base and poly-methyl-methacrylate (PMMA) particulates. Surfaces of the resin polymerized in wet conditions were characterized with PMMA particulates having rougher surfaces suggestive of water incorporation. Raising temperature and pressuring during polymerization increase strength and stiffness of autopolymerizing resin. However, wet condition reduces surface hardness of resin compared with dry condition. These altered mechanical properties are associated with polymerization behaviour of the resin.

Acrylic Resins↗

PubMed1999

Physical-property comparison of a chairside- or laboratory-polymerized permanent soft-liner during 1 year.

PURPOSE: This investigation examined the influence of polymerization mode and water storage duration on the Shore A hardness, water sorption, resin solubility, and glass transition temperature of Permasoft, a commercial soft denture liner that is polymerized either chairside or in the laboratory. MATERIALS AND METHODS: Specimen disks (31-mm diameter x 10 mm thick) and bars (44 x 8.5 x 1.2 mm) were polymerized following manufacturer's recommendations. The chairside polymerization process was simulated by pouring the mixed components into a mold and processing at 70 degrees C for 15 minutes under 2-psi pressure. Laboratory-polymerized specimens of the same dimensions were fabricated by processing under 500-psi pressure at 100 degrees C for 45 minutes. Specimens were stored in distilled water at 37 degrees C for 1, 7, and 30 days, and 6 and 12 months. Specimens were tested for Shore A hardness, water sorption, resin solubility, and glass transition temperature after the prescribed interval. To determine the effects of polymerization mode and storage time on material properties, a repeated-measures ANOVA (hardness data) and a two-way ANOVA (sorption and solubility data) with appropriate post-hoc tests were used. RESULTS: Shore A hardness values increased from a low of 9.4 (+/- 0.5) units immediately after fabrication to a maximum of 15.9 (+/- 1.1) units after 1 year. Mode of polymerization did not influence hardness (p = .9851). Water-sorption values ranged from 4.2 (+/- 0.2%) of dry weight to 14.7 (+/- 2.5%) after 1 year. Resin solubility varied from 10.3 (+/- 0.6%) of preimmersion weight to 15.4 (+/- 1.1%), and immersion duration had no effect on solubility. In addition, after 1 year of storage, no difference in resin solubility or water sorption was found with respect to cure mode. The glass transition temperature for chairside-polymerized samples approximated -10 degrees C, while that for labpolymerized samples approximated -15 degrees C. CONCLUSIONS: With regard to the material properties evaluated in this study, clinically processed Permasoft liner was equivalent to the laboratory-processed material.

Absorption↗

PubMed1985

Polymeric phospholipids as new biomaterials.

Phospholipid polymers form a new class of biomaterials with many potential applications in medicine and research. The development of these compounds is based upon the mimicry of cell surfaces and reflects our current understanding of the properties of membrane lipids. Physicochemical characterization of the monomeric, diacetylenic phospholipids illustrates the similarities to naturally occurring lipids, similarities that are confirmed by the capacity to enrich the membranes of A. laidlawii to the level of 90% diacetylenic lipid. Polymerization of diacetylenic phospholipids is easily attained by irradiation and produces a stable, crystalline array. The ability to link membrane lipids covalently permits the isothermal restriction in their motion, and is useful in basic studies of biomembranes. The thromboresistance of polymeric phosphatidylcholines in vitro may be a consequence of the inability of phosphatidylcholines to participate in coagulation. The restricted lateral diffusion of proteins along a polymeric lattice will also inhibit the formation of coagulation complexes. Existing polymers may be altered by a coating of polymeric lipid obtained by the Langmuir-Blodgett method. Polymerized vesicles display significant reductions in permeability and aggregation. Entrapment of soluble materials and reconstitution of membrane proteins may be exploited in controlled and site-directed drug delivery. Polymerization of cells in situ produces "cellular capsules" with entrapped membrane and cellular components. Polymeric hemosomes are capable of gas transport and may function as red cell surrogates. The hybrid qualities of biomembranes (polar surfaces, nonthrombogenic, low antigenic potential, and low permeability) and synthetic polymers (chemical and physical stability) suggest that polymeric phosphatidylcholines may serve as models for biomaterials design.

Acetylene↗

PubMed2003

Estradiol and testosterone have opposite effects on microtubule polymerization.

We have reported earlier the purification of tubulin from a plasmalemmal-microsomal fraction derived from rat hippocampus using an estradiol (E(2)) affinity column and the specific binding of tubulin to both E(2) and testosterone (T). To further investigate the effect of E(2) and T on the function of this protein, changes in microtubule polymerization as a result of exposure to the steroids were examined in this study, using both pure tubulin and rat hippocampal primary cell cultures. First, pure tubulin was incubated with or without steroids for 30 min on ice followed by polymerization at 37 degrees C. The numbers of microtubules formed were counted from electron microscopic pictures. The results showed that at 30 min of polymerization, 10 nM, 30 nM and 30 microM of E(2) inhibited microtubule assembly by -70%, -94%, and -92%, respectively (p < 0.01), while T at the same three concentrations stimulated it by +83%, +66%, and +121%, respectively (p < 0.05). The inhibitory effect of E(2) and the stimulatory effect of T were observed at 15, 30 and 60 min of the polymerization process. Next, primary cell cultures from 17-day rat fetus hippocampal tissues were treated with the steroids and polymerized microtubules (Triton X-100 resistant) were examined by immunocytochemistry. The results demonstrated that 60 min of E(2) treatment (10 nM) decreased the intensity of the immunolabeling of polymerized microtubules. The effect of T at nM concentration was not significant though it increased the immunolabeling at microM concentration. Of great significance was a remarkable inhibition by T of the well-established depolymerization effect of colchicine in both the pure tubulin assay and the cell culture model, while E(2) was not effective. In an effort to pursue the possible mechanism(s) of the effect of E(2) and T on microtubule formation, we found that T only inhibited the microtubule depolymerization process without affecting the rate of polymerization. In contrast, E(2) modifies only the polymerization process without altering the depolymerization. Overall, these data indicate that E(2) and T may be considered as novel regulators of microtubule dynamics and thereby controlling cytoskeleton function in cells.

Analysis of Variance↗

PubMed2006

A polymeric micelle system with a hydrolysable segment for drug delivery.

A potential anti-cancer drug-delivery polymeric micelle system with an in vitro degradation half-life of about 48 h that releases its drug upon application of ultrasound was synthesized. This vehicle was composed of an amphiphilic co-polymer, poly(ethylene oxide)-b-poly(N-isopropylacrylamide-co-2-hydroxyethyl methacrylate-lactate(n)). The degree of polymerization of the lactate side group, n, was 0, 3 or 5. The molar ratio of NIPAAm to HEMA-lactate(n) to PEO in polymerization was optimized to produce an in vitro polymeric micelle half-life of about 48 h at 40 degrees C. 1,6-Diphenyl-1,3,5-hexatriene (DPH) was used as a fluorescent probe to study the hydrophobicity of the cores of the polymeric micelles. The results showed that the cores of the polymeric micelles were hydrophobic enough to sequester DPH and the anti-cancer drug doxorubicin (Dox). Dox was encapsulated into the polymeric micelles having a molar feed ratio of NIPAAm to HEMA-lactate3 to PEO equal to 20:5:1; this drug was released upon the application of low-frequency ultrasound. The Dox release was about 2% at room temperature and 4% at body temperature, and the drug returned to the polymeric micelles when insonation ceased.

Acrylic Resins↗

PubMed1972

Platelet interaction with polymerizing fibrin.

Interaction of washed pig, rabbit, or human platelets with fibrinogen was studied during its transition to fibrin using photometric, isotopic, and electron microscopic techniques. Untreated fibrinogen and fully polymerized fibrin had no detectable effect on platelets. Fibrinogen, incubated with low concentrations of reptilase or thrombin, formed intermediate products which readily became associated with platelets and caused their aggregation. Neutralization of the thrombin did not prevent this interaction. In the absence of fibrinogen, reptilase did not affect platelets. The interaction of polymerizing fibrin with platelets was accompanied by small losses of platelet constituents (serotonin, adenine nucleotides, platelet factor 4, and lactic dehydrogenase). This loss did not appear to be the result of the platelet release reaction. Inhibitors of the release reaction or of adenosine diphosphate (ADP)-induced aggregation did not prevent the interaction of platelets with polymerizing fibrin. Apyrase or prostaglandin E(1) (PGE(1)) reduced the extent of platelet aggregation by polymerizing fibrin, but the amount of protein associated with platelets was slightly increased. The interaction of polymerizing fibrin with platelets was completely inhibited by ethylenediaminetetraacetate (EDTA) or ethylene glycol bis (beta-aminoethyl ether) N, N,N',N'-tetraacetic acid (EGTA).Fibers formed in solutions of polymerizing fibrin were larger in the presence than in the absence of washed platelets, suggesting that platelets affect fibrin polymerization. The adherence of platelets to polymerizing fibrin may be responsible for the establishment of links between platelets and fibrin in hemostatic plugs and thrombi.

Adenine Nucleotides↗

PubMedDate not supplied

Shrinkage stress of three composites under different polymerization methods.

The aim of this study was to evaluate the shrinkage stress of three composites under different polymerization methods: halogen conventional polymerization (G1), halogen "soft-start" polymerization (G2) and LED polymerization (G3). The composites tested were Filtek Z-100 (3M/ESPE), Filtek Z-250 (3M/ESPE) and Solitaire 2 (Heraeus Kulzer). For G1, an XL-3000 (3M/ESPE) curing unit with light intensity of 507 mW/cm2 was employed. In G2, the same light unit was used, but with a reduced light intensity in the first 20 s (166 mW/cm2). In G3, an Ultrablue I (DMC) LED curing unit with light intensity of 125 mW/cm2 was used. The test was performed with a DL 2000 (EMIC) universal testing machine and two metallic molds with a 1 mm space between them. The composites were inserted in the space between the molds and light cured according to the protocols mentioned above. Stress was registered in different periods of time: 10, 20, 40, 60, 90 and 120 s. A significant linear increase of the shrinkage stress over time was observed, except for Z-100 in G2. Generally, LED polymerization (G3) reduced the generated stress when compared to conventional halogen polymerization (G1). In G3, the composite with the additional co-initiator presented lower stress when compared to the other composites tested. The combination between composite and polymerization method produced different patterns of stress behavior. LED polymerization reduced the initial shrinkage stress of the three materials and was influenced by the presence of co-initiators in the composites.

Analysis of Variance↗

PubMed2005

Polymeric gene carriers.

Polymeric gene carriers are a potential alternative to using viral vectors. Polymeric carriers have relatively low immunogenicity and cytotoxicity. In addition, polymeric carriers can accommodate large-size DNA, be conjugated with appropriate functionalities, and be administered repeatedly. In spite of these advantages, polymeric gene carriers have some limitations, such as low gene transfection efficiencies and relatively short duration of gene expression. Therefore, extensive research has been conducted toward the development of efficient polymeric carriers. In this review, we discuss current problems associated with polymeric gene carriers and various strategies against transfection barriers in particular, gene stabilization and protection, cellular targeting, endosomal escaping, nuclear targeting, unpackaging, and biocompatibility. Finally, requirements for future polymeric gene carriers are considered. With all these ongoing efforts, polymeric carriers have become one of the promising gene delivery methods for human gene therapy.

Animals↗