SEARCH · Search PubMed

Results for “Polymerization”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

SourceResearch connectionFrom yearThrough year

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 649 records · Page 36Linked to original sources

PubMed2004

Tamoxifen-loaded polymeric micelles: preparation, physico-chemical characterization and in vitro evaluation studies.

Several samples of polymeric micelles, formed by amphiphilic derivatives of PHEA, obtained by grafting into polymeric backbone of PEGs and/or hexadecylamine groups (PHEA-PEG-C(16) and PHEA-C(16)) and containing different amount of Tamoxifen, were prepared. All Tamoxifen-loaded polymeric micelles showed to increase drug water solubility. TEM studies provided evidence of the formation of supramolecular core/shell architectures containing drug, in the nanoscopic range and with spherical shape. Samples with different amount of encapsulated Tamoxifen were subjected to in vitro cytotoxic studies in order to evaluate the effect of Tamoxifen micellization on cell growth inhibition. All samples of Tamoxifen-loaded polymeric micelles showed a significantly higher antiproliferative activity in comparison with free drug, probably attributable to fluidification of cellular membranes, caused by amphiphilic copolymers, that allows a higher penetration of the drug into tumoral cells. To gain preliminary information about the potential use of prepared micelles as Tamoxifen drug delivery systems, studies evaluating drug release ability of micelle systems in media mimicking biological fluids (buffer solutions at pH 7.4 and 5.5) and in human plasma were carried out. These studies, performed evaluating the amount of Tamoxifen that remains in solution as a function of time, showed that at pH 7.4, as well as in plasma, PHEA-C(16) polymeric micelles were able to release lower drug amounts than PHEA-PEG(5000)-C(16) ones, while at pH 5.5, the behavior difference between two kind of micelles was less pronounced.

Antineoplastic Agents, Hormonal↗

PubMed2005

Enzymatic polymerization behavior using cellulose-binding domain deficient endoglucanase II.

A mutant enzyme, EGII(core), in which the cellulose-binding domain was deleted from endoglucanase II from Trichoderma viride, was expressed in yeast, and the secreted enzyme was examined for the enzymatic polymerization to obtain artificial cellulose. EGII(core) polymerized beta-cellobiosyl fluoride to afford crystalline cellulose of type II. Comparison of the polymerization behavior of EGII(core) with that of EGII revealed the following: i) the crystalline product obtained with EGII(core) was stable in the polymerization solution, although the product was readily hydrolyzed in the presence of EGII; ii) the turnover number of EGII(core) was as high as that of EGII; iii) EGII(core) produced highly crystalline cellulose. EGII(core) is therefore advantageous for enzymatic polymerization.

Cellobiose↗

PubMed2006

Real-time analysis of enzymatic surface-initiated polymerization using surface plasmon resonance (SPR).

The kinetics of enzymatic surface-initiated polymerization of PHB on gold surface has been examined by SPR and the resultant polymer layers characterized by AFM and FT-IR spectrometry. The immobilized enzyme catalyzed surface-initiated polymerization of 3HB-CoA, resulting in the formation of a polymer brush on the surface. The rate of polymer growth from the surface was monitored by SPR in real-time. Polymer growth as measured by the increase in the resonance angle showed no apparent lag phase during the polymerization reaction. SPR analysis also revealed that the thickness of the polymer film could be controlled by varying the initial enzyme density on the surface. The average thicknesses of the PHB film after polymerization reaction were 95, 45 and 15 nm for the surfaces that were treated with 0.5, 0.3 and 0.1*10(-6) M of enzyme, respectively. The binding of PHA synthase at different concentration to the mixed SAMs and subsequent polymerization.

Acyltransferases↗

PubMedDate not supplied

A new method for the preparation of polymeric porous layer open tubular columns for GC application.

A new method to prepare polymeric PLOT columns by using in situ polymerization technology is described. The method involves a straightforward in situ polymerization of the monomer. The polymer produced is directly coated on the metal tubing. This eliminates many of the steps needed in conventional polymeric PLOT column preparation. Our method is easy to operate and produces very reproducible columns, as shown previously (T. C. Shen. J. Chromatogr. Sci. 30, 239, 1992). The effects of solvents, tubing pretreatments, initiators and reaction temperatures in the preparation of PLOT columns are studied. Several columns have been developed to separate (1) highly polar compounds, such as water and ammonia or water and HCN, and (2) hydrocarbons and inert gases. A recent improvement has allowed us to produce bonded polymeric PLOT columns. These were studied, and the results are included also.

Chromatography, Gas↗

PubMed1993

Actin polymerization in boar spermatozoa: fertilization is reduced with use of cytochalasin D.

The aggregational state of actin in boar spermatozoa after capacitation and the acrosome reaction has been examined by several methods. In vitro fertilization (IVF) experiments were conducted in the presence and absence of cytochalasin D (CD) to evaluate the role of actin polymerization in the events of fertilization. The fertilizing capacity was very high in controls, but, when CD (an inhibitor of the polymerization of actin) was added to the capacitation medium, there was a marked decrease in the fertilizing capacity of the boar spermatozoa. There was a further decrease when CD was present during both capacitation and fertilization processes. In addition to the IVF tests, biochemical and immunoelectron microscopic methods were used to analyze the state of aggregation of actin in boar spermatozoa after capacitation, and the acrosome reaction. By immunoelectron microscopy with a phalloidin probe, there were no gold particles, indicating the presence of F-actin on boar sperm heads capacitated and acrosome-reacted in media containing CD. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis there were differences in NP-40 solubility, reflecting actin polymerization, between CD-treated and untreated sperm. These results suggest that actin polymerizes during capacitation and the acrosome reaction and that this polymerization is essential to the fertilization process.

Acrosome↗

PubMedDate not supplied

Quantitative analysis of polymeric proanthocyanidins in birch leaves with normal-phase HPLC.

The proanthocyanidin composition and content in the leaves of nine birch species (Betula albosinensis, B. ermanii B. maximowicziana, B. nana, B. papyrifera, B. pendula, B. platyphylla, B. pubescens, and B. pubescens ssp. czerepanovii) were studied with different methods including colorimetric assay, HPLC coupled with PAD or ESI/MS and NMR. Total proanthocyanidin content was determined using the acid butanol assay. A normal phase-HPLC method was applied for the analysis of polymeric proanthocyanidins. The content of polymeric proanthocyanidins was estimated from a late eluting peak in the chromatogram. With this HPLC method, quantitative analysis of polymeric proanthocyanidins could be performed directly from leaf extracts: no additional purification or preparation steps were required. It was shown that birch leaves contained mainly polymeric proanthocyanidins with a degree of polymerisation greater than 10. Total proanthocyanidin content (expressed as dry weight) was found to vary from 44mg/g (B. papyrifera) to 145mg/g (B. nana), and polymeric proanthocyanidin content from 39mg/g (B. pendula) to 119 mg/g (B. nana).

Betula↗

PubMed1995

Polymerization of an Escherichia coli elongation factor Tu.

Elongation factor Tu (EF-Tu) from Escherichia coli is shown here to polymerize under conditions of low ionic strength and slightly acidic pH. Several factors, such as decreasing pH, decreasing ionic strength, increasing temperature, and increasing protein concentration (up to 2.5 microM) enhance the rate of polymerization. Both EF-Tu.GTP and EF-Tu.GDP polymerized equally well under the conditions studied. A lag time was observed between the lowering of the pH and the onset of measurable polymerization, which was not overcome by addition of preformed polymer "seeds." Finally, addition of unpolymerized EF-Tu.GDP to a solution of polymerized EF-Tu.GDP appears to lead to formation of new polymers instead of addition to preexisting ones, which may suggest a size limit for polymers of EF-Tu.GDP.

Escherichia coli↗

PubMed1998

The mechanism of alpha 1-antitrypsin polymerization probed by fluorescence spectroscopy.

The polymerization of alpha1-antitrypsin within the hepatic cell leads to alpha1-antitrypsin deficiency. Both the conformational changes and the kinetics of the polymerization process are poorly understood. Here we describe fluorescence experiments investigating the polymerization reaction using the fluorescent probe4, 4'-dianilino-1,1'-binaphthyl-5,5'-disulfonate (bis-ANS) which bound to both native and polymerized alpha1-antitrypsin. Biphasic changes in bis-ANS fluorescence were observed during formation of alpha1-antitrypsin polymers. Initially a rapid increase in fluorescence signal was observed; it was followed by a gradual reduction in fluorescence signal. The first phase is a conformational change in which the A beta-sheet of alpha1-antitrypsin opens, whereas the second phase represents the insertion of the reactive center loop into the A beta-sheet of another molecule and therefore determines the rate of the polymerization process.

Biopolymers↗

PubMed1998

Chemical and Photochemical Dual Polymerization in a Mixed Langmuir Monolayer of Diacetylene Derivatives and Octadecyltrimethoxysilane.

A chemical-and-photochemical-induced dual polymerization at the air-water interface was performed for the first time, by using a ternary mixture of a octadecyltrimethoxysilane (C18TMS), 10,12-pentacosadiynoic acid (PDA), and N-(11-O-alpha-d-mannopyranosyl-3,6,9-trioxa) undecyl 10,12-pentacosa-diynamide (PDTM). Different dual polymerization behaviors of the mixed monolayers of PDA/PDTM/C18TMS (7:1:8 molar ratio) at different subphase pH were monitored by surface pressure-area isotherms and UV-vis spectra. At pH 1, the C18TMS formed a long linear polymer network by strong intermolecular condensation. The PDA/PDTM was isolated to small domains by this network and can only be polymerized weakly upon UV irradiation. At pH 2.6, the weak condensation of C18TMS formed short linear polymers, which caused phase separation between C18TMS and PDA/PDTM. The strong photochemical polymerization of the PDA/PDTM rich domain was similar to the PDA/PDTM binary mixed monolayer. At pH 4.0, the partially hydrolyzed C18TMS was miscible with PDA/PDTM and slowed the polymerization process of PDA/PDTM upon UV irradiation. These results show geometry and kinetic controls of the PDA/PDTM polymer in 2D by using the C18TMS polymer network. Copyright 1998 Academic Press.

Journal Article↗

PubMed2002

Formation of monodisperse polyacrylamide particles by radiation-induced dispersion polymerization: particle size and size distribution.

Polyacrylamide microparticles were directly produced by radiation-induced dispersion polymerization in aqueous alcohol media using poly(N-vinylpyrrolidone) as a steric stabilizer at room temperature. The hydrodynamic diameter of a polymer particle and its distribution were measured on a dynamic laser light-scattering spectrometer. This method takes advantages of the specialties of radiation induction, and highly uniform polymer microspheres were obtained with high conversion. The number of the particle produced in the early stage of the polymerization was found to be constant during the remainder of the polymerization. The effects of various polymerization parameters, such as absorbed dose rate, monomer concentration, stabilizer content, medium polarity, and polymerization temperature on the particle size and size distribution were systematically investigated.

Journal Article↗

PubMed1997

Conformational flexibility and polymerization of vesicular stomatitis virus matrix protein.

The matrix protein of vesicular stomatitis virus (VSV) plays a pivotal role in viral assembly. We previously demonstrated the ability of M protein to self-associate at low salt concentrations. Now, we show the ability of M protein to polymerize in the presence of ZnCl2 in a nucleation-dependent manner. Analysis of kinetics revealed that the nuclei are probably made of three or four molecules of M. These results are consistent with the idea that in vitro self association of M protein is not due to amorphous aggregation but rather reflects an intrinsic ability of M to polymerize. Using attenuated total reflectance Fourier transform infrared spectroscopy, we showed that M polymerization is associated with an increase in the beta-sheet content of the protein. We propose a model explaining both the apparent M protein solubility in infected cells and how M polymerization could promote viral assembly. Data available for other negative strand viruses suggest that M polymerization may be the general basis of viral assembly.

Chlorides↗

PubMed1999

Computer simulations of actin polymerization can explain the barbed-pointed end asymmetry.

Computer simulations of actin polymerization were performed to investigate the role of electrostatic interactions in determining polymerization rates. Atomically detailed models of actin monomers and filaments were used in conjunction with a Brownian dynamics method. The simulations were able to reproduce the measured barbed end association rates over a range of ionic strengths and predicted a slower growing pointed end, in agreement with experiment. Similar simulations neglecting electrostatic interactions indicate that configurational and entropic factors may actually favor polymerization at the pointed end, but electrostatic interactions remove this trend. This result would indicate that polymerization at the pointed end is not only limited by diffusion, but faces electrostatic forces that oppose binding. The binding of the actin depolymerizing factor (ADF) and G-actin complex to the end of a filament was also simulated. In this case, electrostatic steering effects lead to an increase in the simulated association rate. Together, the results indicate that simulations provide a realistic description of both polymerization and the binding of more complex structures to actin filaments.

Actin Cytoskeleton↗

PubMed2000

Interspecies hybrid HbS: complete neutralization of Val6(beta)-dependent polymerization of human beta-chain by pig alpha-chains.

Interspecies hybrid HbS (alpha(2)(P)beta(2)(S)), has been assembled in vitro from pig alpha-globin and human beta(S)-chain. The alpha(2)(P)beta(2)(S) retains normal tetrameric structure (alpha(2)beta(2)) of human Hb and an O(2) affinity comparable to that of HbS in 50 mM Hepes buffer; but, its O(2) affinity is slightly higher than that of HbS in the presence of allosteric effectors (chloride, DPG and phosphate). The (1)H-NMR spectroscopy detected distinct differences between the heme environments and alpha(1)beta(1) interfaces of pig Hb and HbS, while their alpha(1)beta(2) interfaces appear very similar. The interspecies hybrid alpha(2)(H)beta(2)(P) resembles pig Hb; the pig beta-chain dictated the conformation of the heme environment of the human alpha-subunit, and to the alpha(1)beta(1) interfaces of the hybrid. In the alpha(2)(P)beta(2)(S) hybrid, beta(S)-chain dictated the conformation of human heme environment to the pig alpha-chain in the hybrid; but the conformation of alpha(1)beta(1) interface of this hybrid is close to, but not identical to that of HbS. On the other hand, the alpha(1)beta(2) interface conformation is identical to that of HbS. More important, the alpha(2)(P)beta(2)(S) does not polymerize when deoxygenated; pig alpha-chain completely neutralizes the beta(S)-chain dependent polymerization. The polymerization inhibitory propensity of pig alpha-chain is higher when it is present in the cis alpha(P)beta(S) dimer relative to that in a trans alpha(P)beta(A) dimer. The semisynthetically generated chimeric pig-human and human-pig alpha-chains by exchanging the alpha(1-30) segments of human and pig alpha-chains have established that the sequence differences of pig alpha(31-141) segment can also completely neutralize the polymerization. Comparison of the electrostatic potential energy landscape of the alpha-chain surfaces of HbS and alpha(2)(P)beta(2)(S) suggests that the differences in electrostatic potential energy surfaces on the alpha-chain of alpha(2)(P)beta(2)(S) relative to that in HbS, particularly the ones involving CD region, E-helix and EF-corner of pig alpha-chain are responsible for the polymerization neutralization activity. The pig and human-pig chimeric alpha-chains can serve as blueprints for the design of a new generation of variants of alpha-chain(s) suitable for the gene therapy of sickle cell disease.

Allosteric Regulation↗

PubMed2002

Effect of hemoglobin polymerization on oxygen transport in hemoglobin solutions.

The effect of hemoglobin (Hb) polymerization on facilitated transport of oxygen in a bovine hemoglobin-based oxygen carrier was studied using a diffusion cell. In high oxygen tension gradient experiments (HOTG) at 37 degrees C the diffusion of dissolved oxygen in polymerized Hb samples was similar to that in unpolymerized Hb solutions during oxygen uptake. However, in the oxygen release experiments, the transport by diffusion of dissolved oxygen was augmented by diffusion of oxyhemoglobin over a range of oxygen saturations. The augmentation was up to 30% in the case of polymerized Hb and up to 100% in the case of unpolymerized Hb solution. In experiments performed at constant, low oxygen tension gradients in the range of physiological significance, the augmentation effect was less than that in the HOTG experiments. Oxygen transport in polymerized Hb samples was approximately the same as that in unpolymerized samples over a wide range of oxygen tensions. However, at oxygen tensions lower than 30 mm Hg, there were more significant augmentation effects in unpolymerized bovine Hb samples than in polymerized Hb. The results presented here are the first accurate, quantitative measurements of effective diffusion coefficients for oxygen transport in hemoglobin-based oxygen carriers of the type being evaluated to replace red cells in transfusions. In all cases the oxygen carrier was found to have higher effective oxygen diffusion coefficients than blood.

Animals↗

PubMed1985

Time-resolved X-ray scattering study of actin polymerization from profilactin.

The polymerization of actin in solutions of purified calf spleen actin or profilactin (1-10 mg . ml-1) was followed by synchrotron radiation X-ray solution scattering. At the concentration used, polymerization of actin from profilactin or actin occurs without any lag phase. It is shown by a combination of solution scattering, model calculations and electron microscopy that contrary to the conclusions from previous viscometry studies, filaments form without any lag phase in profilactin solution but aggregate in bundles or networks. This phenomenon is independent of the method used to induce polymerization: slow temperature increase, temperature jump in the presence of polymerizing salts or fast mixing with salt. This aggregation explains the lower final viscosity levels, as compared to actin solutions, observed during the polymerization of actin from profilactin.

Actins↗

PubMed1987

Facilitation of actin polymerization by interfilamentous factors.

The polymerization of actin in low ionic strength buffer at 0 degrees C in the presence of 0.25 mM Mg2+ was studied by viscometry, turbidity and absorbance at 232 nm. Under these conditions, significant polymerization occurred only in the viscometer and not in isotropic mixtures. The polymerization rate with 0.25 mM MgCl2, as judged from shear viscosity, was equal to or greater than that observed with 0.1 M KCl and 0.25 mM MgCl2 at 0 degrees C, and was characterized by a longer nucleation period. Measurements of the turbidity at 350 nm (detecting filament formation and aggregation) and the absorbance at 232 nm (detecting conformational changes of the G-F transition) showed no evidence for polymerization or nucleation in a bulk solution at 0 degrees C when Mg2+ was added to 0.25 mM and, furthermore, F-actin nuclei were ineffective as seeds under these conditions. However, nucleation and polymerization by these criteria could be induced by raising the temperature to 20 degrees C. These results demonstrate the existence of narrow conditions when elongation of F-actin is dissociated from nucleation of oligomeric acceptor nuclei, even if monitored on the sub-molecular level (absorbance at 232 nm). Under these conditions, elongation appears to require anisotropic F-actin, i.e. that filaments are ordered by laminar flow.

Actins↗

PubMed1996

Fluorescence-detected polymerization kinetics of human alpha 1-antitrypsin.

The time dependence of the human alpha 1-antitrypsin polymerization process was studied by means of the intrinsic fluorescence stopped-flow technique as well as the fluorescence-quenching-resolved spectra (FQRS) method and native PAGE. The polymerization was induced by mild denaturing conditions (1 M GuHCl) and temperature. The data show that the dimer formation reaction under mild conditions was followed by an increase of fluorescence intensity. This phenomenon is highly temperature sensitive. The structure of alpha 1-antitrypsin dimer resembles the conformation of antithrombin III dimer. In the presence of the denaturant the polymerization process is mainly limited to the dimer state. The alpha 1-antitrypsin activity measurements confirm monomer-to-dimer transition under these conditions. These results are in contrast to the polymerization process induced by temperature, where the dimer state is an intermediate step leading to long-chain polymers. On the basis of stopped-flow and electrophoretic data it is suggested that both C-sheet as well as A-sheet mechanisms contribute to the polymerization process under mild conditions.

Dimerization↗

PubMed2003

A polymeric micellar carrier for the solubilization of biphenyl dimethyl dicarboxylate.

A polymeric micelle drug delivery system was developed to enhance the solubility of poorly-water soluble drug, biphenyl dimethyl dicarboxylate, DDB. The block copolymers consisting of poly(D,L-lactide) (PLA) as the hydrophobic segment and methoxy poly(ethylene glycol) (mPEG) as the hydrophilic segment were synthesized and characterized by NMR, DSC and MALDI-TOF mass spectroscopy. The size of the polymeric micelles measured by dynamic light scattering showed a narrow monodisperse size distribution with the average diameter less than 50 nm. The MW of mPEG-PLA, 3000 (MW of mPEG, 2 K; MW of PLA, 1 K), and the presence of hydrophilic and hydrophobic segments on the polymeric micelles were confirmed by MALDI-TOF mass spectroscopy and NMR, respectively. Polymeric micelle solutions of DDB were prepared by three different methods, i.e. the matrix method, emulsion method and dialy-sis method. In the matrix method, DDB solubility was reached to 13.29 mg/mL. The mPEG-PLA 2K-1 K micelle system was compared with the poloxamer 407 micelle system for their critical micelle concentration, micelle size, solubilizing capacity, stability in dilution and physical state. DDB loaded-polymeric micelles prepared by the matrix method showed a significantly increased aqueous solubility (>5000 fold over intrinsic solubility) and were found to be superior to the poloxamer 407 micelles as a drug carrier.

Calorimetry, Differential Scanning↗