Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0344329 (collapse)
 28,634 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Poly(N-isopropylacrylamide) (NIPAAm)/polytetramethylene ether glycol (PTMEG) interpenetrating polymer networks (IPNs) were synthesized and their feasibility as thermosensitive hydrogels for drug release was investigated. The release of indomethacin incorporated into these matrices showed pulsatile patterns in response to temperature changes and was sensitive to a few degrees of temperature fluctuation. The temperature inducing on-off release deviated from the gel collapse temperature of unloaded gel, possibly because of solute effects on network properties. The lag time and release profile of indomethacin in the low-temperature region (on process) of each temperature cycle were affected by the gel composition and applied temperature. The results of this study demonstrate that solute release can be regulated by rapid deswelling of the surface of the gels in response to temperature.
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PMID:"On-off" thermocontrol of solute transport. II. Solute release from thermosensitive hydrogels. 186 77

The swelling in water, as a function of temperature, of two series of N-isopropylacrylamide (NIPAAm) polymer networks was studied. In the first series, n-butylmethacrylate (BMA) was copolymerized with NIPAAm, and in the second, polytetramethylene ether glycol (PTMEG) was incorporated into NIPAAm network as a chemically independent interpenetrating network. With increasing BMA content in the poly(NIPAAm-co-BMA) network, the gel collapse point was lowered and the gels deswelled in a more gradual manner with increasing temperature. In the interpenetrating polymer networks (IPN) system, the gel collapse point was not significantly changed by the amount of incorporated PTMEG. In DSC thermograms of swollen samples, the shape and onset temperature of the endothermic peak corresponded to the gel deswelling behavior and gel collapse point. The temperature dependence of equilibrium swelling in water was shown to be a function of the gel composition in both network series. The synthesized networks formed a dense surface layer as the temperature increased past the gel collapse point. This dense layer retarded water efflux and thereby resulted in water pockets at the membrane surface.
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PMID:"On-off" thermocontrol of solute transport. I. Temperature dependence of swelling of N-isopropylacrylamide networks modified with hydrophobic components in water. 187 Oct 53

The enzyme beta-galactosidase has been immobilized within thermally reversible hydrogel beads that exhibit LCST (lower critical solution temperature) behavior. The hydrogel beads containing the immobilized enzymes swell and expand below the LCST and deswell and shrink above the LCST. This behavior is reversible. The enzyme was physically entrapped in a crosslinked hydrogel of a copolymer of N-isopropylacrylamide (NIPAAm) and acrylamide (AAm), and formed as beads in an inverse suspension polymerization. The beads were placed in a packed bed column reactor which was operated in a continuous, single pass mode, either isothermally at 30 or 35 degrees C, or with temperature cycling between 30 and 35 degrees C. The thermal cycling significantly enhanced overall reactor enzyme activity relative to isothermal operation at either the higher or lower temperature. It is postulated that mass transfer rates within the hydrogel beads are greatly enhanced by the movement of water in and out of the beads during the expansion or collapse of the polymer chain network as temperature is cycled.
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PMID:Effect of temperature cycling on the activity and productivity of immobilized beta-galactosidase in a thermally reversible hydrogel bead reactor. 314 42

Cross-linked, poly(N-isopropylacrylamide) gel was used to concentrate avian influenza virus from allantoic fluid. Placing the gel in virus-infected allantoic fluid at 4 degrees C caused the gel to swell and absorb small molecular weight solutes, while excluding avian influenza virus and other large particles. Warming the gel to 37 degrees C or more caused the gel to collapse. The gel remained functional after sterilization in an autoclave and could be reused to concentrate other samples of allantoic fluid. Using a combined concentration and elution technique, we were able to achieve an average of 84.2% virus recovery, while reducing the fluid volume from 90 ml to 7.6 ml.
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PMID:Use of temperature-sensitive gel for concentration of influenza virus from infected allantoic fluids. 380 29

The interactions of small unilamellar vesicles (SUV) and water-soluble copolymers were studied by fluorescence spectroscopy, differential scanning calorimetry (DSC) and quasi-elastic light scattering (QELS). The anchoring onto liposomal bilayer membranes of copolymers of N-isopropylacrylamide, N-(2-(1-naphthyl)ethyl)-N-n-octadecylacrylamide and or N-[4-(1-pyrenyl)butyl]-N-n-octadecylacrylamide (0.5 mol% of the octadecylacrylamide comonomer) was monitored by non-radiative energy transfer between excited naphthalene and pyrene. The anchoring process occurred on zwitterionic lecithin liposomes and on negatively charged phosphatidic acid liposomes, whether the bilayer was in the crystalline or the liquid-crystalline phase. Insertion of the copolymer octadecyl groups within crystalline bilayers was attributed to the presence of packing defects. Aqueous solutions of poly-(N-isopropylacrylamide) and of its hydrophobically-modified copolymers exhibit a lower critical solution temperature (LCST). The coil to globule collapse of the polymer chains which is known to occur as the aqueous solution is heated through the LCST, also took place when the copolymers were anchored onto vesicular bilayers. The copolymers remained anchored during this collapse and the liposomes were not destroyed. The process was thermo-reversible. Detailed aspects of the reversibility of the phenomenon depended on the relative values of the phase transition temperatures of the liposomes and of the polymer LCST.
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PMID:Interactions of liposomes and hydrophobically-modified poly-(N-isopropylacrylamides): an attempt to model the cytoskeleton. 827 4

The effect of temperature on kinetic and equilibrium parameters of urea hydrolysis catalyzed with urease immobilized into a thermosensitive poly-N-isopropylacrylamide gel was studied. The temperature behavior of the gel-urease system is different from similar systems. After a decrease in the enzyme activity above the critical temperature, the maximal rate of the enzymatic reaction and gel swelling ratio begin to increase. Urea hydrolysis catalyzed with immobilized urease and shrinking-swelling of the thermosensitive urease-containing gel depend on each other. Under collapse, gel swelling increases due to the enzymatic reaction. The rate of the enzymatic reaction no longer follows Michaelis-Menten kinetics, and the dependence of the reaction rate on substrate concentration becomes more complicated.
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PMID:Relationship between state of a thermosensitive matrix and the activity of urease immobilized in it. 927 75

Novel temperature-sensitive polymers containing glucose units in their backbone were synthesized and covalently conjugated to trypsin. A series of copolymers based on N-isopropylacrylamide (NIPAAm) and glucosyoxylethyl methacrylate (GEMA) were prepared by using 4,4'-azobis(4-cyanovaleric acid) as an initiator, which resulted in one terminal carboxylic acid group per polymer chain. The polymers were conjugated to primary amine groups of trypsin with water-soluble carbodiimide as a coupling agent, which led to a star-shaped conformation. The polymer-enzyme conjugation was confirmed and characterized by size exclusion and reversed-phase chromatography. Almost of all amine groups in trypsin available for the conjugation were consumed and, consequently, a very dense layer of copolymers was actually coated around the enzyme surface. The conjugated enzymes exhibited reversible precipitation/resolubilization behaviors over a wide range of temperatures, depending on the content of GEMA in the copolymer. They also demonstrated no detectable self-digestion (autolysis) process, but the unconjugated enzyme showed very severe autolysis that led to a rapid inactivation in aqueous solution. When bovine serum albumin was used as a substrate, the protein substrate was not attacked by the conjugated enzyme, but completely digested by the unconjugated enzyme. This result was presumably caused by a steric repulsion process of the attached polymer chains around the enzyme toward the protein substrate. However, the enzyme retained sufficient activity against a low molecular weight substrate. Interestingly, the conjugated enzymes demonstrated very peculiar enzyme activity-temperature profiles, with two apparent optimal temperatures, indicating that a temperature-controlled collapse and flocculation of the copolymers around the enzyme surface modulated the mass transfer rates of substrate to the active site of the enzyme. The conjugated enzymes also exhibited improved thermal stability with increasing the amount of carbohydrate units in the polymer chain.
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PMID:Conjugation of trypsin by temperature-sensitive polymers containing a carbohydrate moiety: thermal modulation of enzyme activity. 962 35

A positively thermosensitive drug-release microcapsule (MC) with diameter around 100 microm was designed and its preparation was carried out by using an air suspension coating technique (the Wurster process). The MC had a core layered with carbazochrome sodium sulfonate (CCSS, a water-soluble model drug) particles and a thermosensitive coat composed of an ethylcellulose matrix containing nano-sized thermosensitive hydrogels. The hydrogel particles consisted of a newly synthesized composite latex with a poly(N-isopropylacrylamide (NIPAAm)) shell that could reversibly change the shell thickness in water with response to an environmental temperature change. This MC demonstrated a positively thermosensitive drug release: the release rate was remarkably enhanced at temperatures above a lower gel collapse point (temperature for complete deswelling) of 32 degrees C, suggesting that the shrinkage of poly(NIPAAm) shells most likely created many voids in the coat and thereby imparted the higher water-permeability to the coat. Thermosensitivity of drug release highly depended on the composite latex particle content in the coat. It became most distinct when its content reached 12.5 and 15 wt%. In addition, it was found that the present MC membrane made it possible to obtain an 'on-off' pulsatile release, which could alter the release rate in the order of a minute, in response to stepwise temperature changes between 30 and 50 degrees C.
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PMID:A novel positively thermosensitive controlled-release microcapsule with membrane of nano-sized poly(N-isopropylacrylamide) gel dispersed in ethylcellulose matrix. 1064 May 84

Poly(N-isopropylacrylamide) (PNIPAM) microgel particles dispersed in water have been used as a matrix for the polymerization of a hydrophobic monomer, N-methylpyrrole (MPy). The presence of poly(MPy) (PMPy) within the dried composite particles has been confirmed using electron paramagnetic resonance (EPR) measurements which show a characteristic free-radical signal at g=2.007. Electron microscopy data (TEM) show that the composite PNIPAM-xPMPy particles have a "raspberry-like" morphology. (The value for x represents the volume percent of MPy added during synthesis with respect to the total microgel volume.) PCS data indicate that PMPy occupies the majority of the collapsed composite particle volume. The maximum value of x consistent with colloid stability for PNIPAM-xPMPy dispersions is 4.5%. Higher values of x result in coagulation due to interparticle bridging by PMPy. Variable temperature PCS measurements of the PNIPAM-xPMPy dispersions have been used to study the thermally induced collapse of the composite particles. The extent of collapse becomes less with increasing values for x. The embedded PMPy particles restrict the extent of PNIPAM network contraction. The stability of the PNIPAM-4.5PMPy dispersions was investigated by means of turbidity measurements using aqueous 0.1 M NaCl solution. The upper critical flocculation temperatures (UCFT) for PNIPAM and PNIPAM-4.5PMPy dispersions were identical (38-39 degrees C). The flocculation observed was found to be fully reversible. The composite dispersion stability in the absence of salt was attributed to electrosteric stabilization afforded by the PNIPAM matrix. These results indicate that PNIPAM microgel particles may have application as a matrix for the polymerization of hydrophobic monomers in water. Copyright 2000 Academic Press.
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PMID:Microgel Particles as a Matrix for Polymerization: A Study of Poly(N-isopropylacrylamide)-Poly(N-methylpyrrole) Dispersions. 1065 27

Poly-N-isopropylacrylamide (PNIPAM) is a chemical isomer of poly-leucine, having the polar peptide group in the side-chain rather than in the backbone. It has been demonstrated experimentally that PNIPAM dissolved in aqueous solution undergoes a collapse transition from coil to globule on increasing temperature above the θ-point. By a careful reviewing of existing experimental data, we emphasize that such coil to globule collapse has to be considered an intramolecular first-order transition, analogous to the cold renaturation of small globular proteins. The main theoretical approaches to the coil to globule collapse in homopolymers are discussed briefly, and a critical comparison between the existing models is performed. We point out that, as a general result, the coil to globule collapse is expected to be a first-order transition for rigid and semi-rigid macromolecules. Finally, taking advantage of the analogy between the coil to globule collapse of PNIPAM and the cold renaturation of small globular proteins, we try to clarify some important and intriguing aspects of protein thermodynamics. This leads to the conclusion that the amphiphilic nature of polypeptide chain plays the fundamental role for the existence of two temperature-induced conformational transitions.
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PMID:On the temperature-induced coil to globule transition of poly-N-isopropylacrylamide in dilute aqueous solutions. 1070 90


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