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Suitable Matrix (suitable + matrix)
Selected AbstractsBiocatalytic hydrogels by template polymerizationPOLYMERS FOR ADVANCED TECHNOLOGIES, Issue 5 2008H. El-Sherif Abstract Novel ionizable hydrogels were prepared from poly(acrylic acid) and dimethylaminoethyl methacrylate monomer employing template polymerization technique as an alternative to traditional physical and chemical crosslinking. The mode of interaction, as proved by Fourier Transform Infrared Spectroscopy (FTIR), was multiple H-bonding between the tertiary amino group of the monomer and the carboxylic groups of the polymer. The hydrogels represented suitable matrices for enzyme immobilization. The effect of varying the polymer,monomer molar ratio on the swelling kinetics and parameters was investigated. The dynamic swelling isotherm exhibited a Fickian mode of penetrant sorption and a plateau that increases with the amino group content. A polymer complex of molar ratio (polymer:monomer) 0.5:0.8 had a weight swelling ratio of 10 and 7 at pHs 3 and 8, respectively. The proven pH sensitivity together with the amphoteric character of these hydrogels make them good candidates for another bioapplication such as oral delivery systems of therapeutic peptides and proteins. The structural integrity of the hydrogels was proved by their swelling reversibility. , -Galactosidase, as an acidic model enzyme, was immobilized covalently on the synthesized hydrogels. The maximum enzyme velocity (Vmax) was enhanced to 19,µmol/min/mg, for polycomplex of molar ratio 0.5:0.8, compared with 3.2,µmol/min/mg for the free enzyme. Copyright © 2008 John Wiley & Sons, Ltd. [source] The Influence of Tetracycline Loading on the Surface Morphology and Biocompatibility of Films Made from P(3HB) Microspheres,ADVANCED ENGINEERING MATERIALS, Issue 7 2010Lydia Francis Tetracycline, an antibiotic used against a broad range of Gram positive and Gram negative bacteria was encapsulated in microspheres made of poly(3-hydroxybutyric acid) P(3HB), a microbial biodegradable polymer isolated from Bacillus cereus SPV. The drug loaded microspheres were prepared using an oil emulsion technique and compressed uniaxially to produce films. Although the same fabrication conditions were used for preparing the drug loaded and unloaded microspheres, the presence of the drug changed the surface morphology and roughness of the films. The surface morphology of the drug loaded films appeared uneven and coarser and the roughness, with an average root mean square value of 5.89,µm, was significantly higher than that of the unloaded film. The in vitro biocompatibility of the films was investigated using a human keratinocyte cell line (HaCaT) by comparing cell viability on the films to that on conventional tissue culture plastics. Both films appear to support cell growth but cell attachment and percentage cell viability were greater on the drug loaded films (32% of control) compared to the unloaded film (10% of control), possibly as a result of the non-uniform surface morphology and increased roughness of the drug loaded film. Thus, the above results illustrate that the drug loaded films, in addition to being a suitable matrix for drug delivery, represent an improved substrate for keratinocyte cell attachment. [source] A fast, reproducible and low-cost method for sequence deconvolution of ,on-bead' peptides via ,on-target' maldi-TOF/TOF mass spectrometryJOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 3 2010Giulio A. Amadei Abstract A novel approach to high-throughput sequence deconvolution of on-bead small peptides (MW < 2000 Da) using on-target MALDI-TOF/TOF instrumentation is presented. Short peptides of pentamer and octamer length, covalently attached to TentaGel polystyrene beads through a photolabile linker, were placed onto the MALDI target, apportioned with suitable matrix (2,5-dihydroxybenzoic acid) and then hit with the instrument laser (Nd : YAG, 355 nm). This induced easy and highly reproducible photochemical cleavage, desorption (MS mode) and fragmentation (MS/MS mode). Peptide fragments were identified with a mass accuracy of 0.1 Da of the expected values. This technique significantly accelerates the sequence determination of positive peptide hits obtained from random combinatorial libraries when screening against biological targets, paving the way for a rapid and efficient method to identify molecular imaging ligands specific to pathological targets in cancer and other diseases. Copyright © 2009 John Wiley & Sons, Ltd. [source] A convenient purification and preconcentration of peptides with ,-cyano-4-hydroxycinnamic acid matrix crystals in a pipette tip for matrix-assisted laser desorption/ionization mass spectrometry,JOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 1 2010Helena, ehulková Abstract Peptide samples derived from enzymatic in-gel digestion of proteins resolved by gel electrophoresis often contain high amount of salts originating from reaction and separation buffers. Different methods are used for desalting prior to matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS), e.g. reversed-phase pipette tip purification, on-target washing, adding co-matrices, etc. As a suitable matrix for MALDI MS of peptides, ,-cyano-4-hydroxycinnamic acid (CHCA) is frequently used. Crystalline CHCA shows the ability to bind peptides on its surface and because it is almost insoluble in acidic water solutions, the on-target washing of peptide samples can significantly improve MALDI MS signals. Although the common on-target washing represents a simple, cheap and fast procedure, only a small portion of the available peptide solution is efficiently used for the subsequent MS analysis. The present approach is a combination of the on-target washing principle carried out in a narrow-end pipette tip (e.g. GELoader tip) and preconcentration of peptides from acidified solution by passing it through small CHCA crystals captured inside the tip on a glass microfiber frit. The results of MALDI MS analysis using CHCA-tip peptide preconcentration are comparable with the use of homemade POROS R2 pipette tip microcolumns. Advantages and limitations of this approach are discussed. Copyright © 2009 John Wiley & Sons, Ltd. [source] Oxidative polymerization of N -vinylcarbazole in polymer matrixPOLYMER INTERNATIONAL, Issue 6 2001Belkis Ustamehmeto Abstract A new class of soluble conductive poly(N -vinylcarbazole) (PVCz) compounds has been developed by oxidative matrix polymerization of N -vinylcarbazole (NVCz) by Ce(IV) in the presence of poly(ethylene glycol) (PEG). PEG was found to be a more suitable matrix with which to obtain a stable homogenous ternary complex solution when compared with poly(acrylic acid) (PAA) and poly(vinylpyrrolidone) (PVP). The role of PEG, NVCz and Ce(IV) concentration, order of component addition, the structure of the polymer matrix, molecular weight of polymer and the effect of solvent have been investigated. Obtaining soluble PEG,Ce(III),PVCz ternary complexes was shown by cyclic voltammetric measurements, and the initial rate of formation NVCz cation radicals as calculated using UV,visible spectrophotometry. Advantageously with these soluble complexes, conductivities could be measured both in solution and in the solid state. © 2001 Society of Chemical Industry [source] Polyacrylamide lamination enables mass spectrometry compatible staining and in-gel digestion of proteins separated by agarose IEFPROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 19 2007Jukka Hellman Dr. Abstract Agarose IEF enables the separation of large proteins and protein complexes. A complication of agarose gels attached onto polyester support is the lack of sensitive protein staining methods compatible with protein analysis and identification protocols. In this study, agarose IEF gels were used to separate the proteins, followed by layering the agarose with polyacrylamide. The formed laminate gels were seamless and durable and they were readily detached from the polyester. The gels were amenable to MS compatible staining. The sensitivity obtained with the acidic silver staining method was 20,50,ng/band of myoglobin. Laminated agarose was a suitable matrix for in-gel digestion based generation of tryptic peptides for MALDI-MS. [source] Pharmacokinetics of intravenous and oral midazolam in plasma and saliva in humans: usefulness of saliva as matrix for CYP3A phenotypingBRITISH JOURNAL OF CLINICAL PHARMACOLOGY, Issue 4 2008Bettina Link WHAT IS ALREADY KNOWN ABOUT THE SUBJECT , Midazolam is a frequently used probe drug for CYP3A phenotyping in plasma. Midazolam and its hydroxy-metabolites can be detected in saliva. WHAT THIS STUDY ADDS , The concentrations of midazolam and its hydroxy-metabolites are much lower in saliva than in plasma, but the midazolam concentrations in both matrices show a significant linear correlation. , Saliva appears to be a suitable matrix for CYP3A phenotyping with midazolam, but very sensitive methods are required due to the low concentrations of midazolam and its hydroxy-metabolites. AIMS To compare midazolam kinetics between plasma and saliva and to find out whether saliva is suitable for CYP3A phenotyping. METHODS This was a two way cross-over study in eight subjects treated with 2 mg midazolam IV or 7.5 mg orally under basal conditions and after CYP3A induction with rifampicin. RESULTS Under basal conditions and IV administration, midazolam and 1,-hydroxymidazolam (plasma, saliva), 4-hydroxymidazolam and 1,-hydroxymidazolam-glucuronide (plasma) were detectable. After rifampicin, the AUC of midazolam [mean differences plasma 53.7 (95% CI 4.6, 102.9) and saliva 0.83 (95% CI 0.52, 1.14) ng ml,1 h] and 1,-hydroxymidazolam [mean difference plasma 11.8 (95% CI 7.9 , 15.7) ng ml,1 h] had decreased significantly. There was a significant correlation between the midazolam concentrations in plasma and saliva (basal conditions: r = 0.864, P < 0.0001; after rifampicin: r = 0.842, P < 0.0001). After oral administration and basal conditions, midazolam, 1,-hydroxymidazolam and 4-hydroxymidazolam were detectable in plasma and saliva. After treatment with rifampicin, the AUC of midazolam [mean difference plasma 104.5 (95% CI 74.1, 134.9) ng ml,1 h] and 1,-hydroxymidazolam [mean differences plasma 51.9 (95% CI 34.8, 69.1) and saliva 2.3 (95% CI 1.9, 2.7) ng ml,1 h] had decreased significantly. The parameters separating best between basal conditions and post-rifampicin were: (1,-hydroxymidazolam + 1,-hydroxymidazolam-glucuronide)/midazolam at 20,30 min (plasma) and the AUC of midazolam (saliva) after IV, and the AUC of midazolam (plasma) and of 1,-hydroxymidazolam (plasma and saliva) after oral administration. CONCLUSIONS Saliva appears to be a suitable matrix for non-invasive CYP3A phenotyping using midazolam as a probe drug, but sensitive analytical methods are required. [source] | |||||||||||||