Light-induced cross-linking and post-cross-linking modification of polyglycidol.

The photoinduced radical generation process has received renewed interest due to its economic and ecological appeal. Herein the light-induced cross-linking of functional polyglycidol and its post-cross-linking modification are presented. Linear polyglycidol was first functionalized with a tertiary amine in a two-step reaction. Dimethylaminopropyl functional polyglycidol was cross-linked in a UV-light mediated reaction with camphorquinone as a type II photoinitiator. The cross-linked polyglycidol was further functionalized by quaternization with various organoiodine compounds. Aqueous dispersions of the cross-linked polymers were investigated by means of DLS and zeta potential measurements. Polymer films were evaluated by DSC and XPS.

Folic acid modified clay/polymer nanocomposites for selective cell adhesion.

A folic acid (FA) modified poly(epsilon-caprolactone)/clay nanocomposite (PCL/MMT-(CH2CH2OH)2-FA) resulting in selective cell adhesion and proliferation was synthesized and characterized as a cell culture and biosensing platform. For this purpose, first the FA modified clay (MMT-(CH2CH2OH)2-FA) was prepared by treating the organo-modified clay, Cloisite 30B [MMT-(CH2CH2OH)2] with FA in chloroform at 60 °C. Subsequent ring opening polymerization of ε-caprolactone in the presence of tin octoate (Sn(Oct)2) using MMT-(CH2CH2OH)2-FA at 110 °C resulted in the formation of MMT-(CH2CH2OH)2-FA with an exfoliated clay structure. The structures of intermediates and the final nanocomposite were investigated in detail by FT-IR spectral analysis and DSC, TGA, XRD, SEM and AFM measurements. The combination of FA, PCL and clay provides a simple and versatile route to surfaces that allows controlled and selective cell adhesion and proliferation. FA receptor-positive HeLa and negative A549 cells were used to prove the selectivity of the modified surfaces. Both microscopy and electrochemical sensing techniques were applied to show the differences in cell adherence on the modified and pristine clay platforms. This approach is expected to be adapted into various bio-applications such as 'cell culture on chip', biosensors and design of tools for targeted diagnosis or therapy.

Various applications of immobilized glucose oxidase and polyphenol oxidase in a conducting polymer matrix.

In this study, glucose oxidase and polyphenol oxidase were immobilized in conducting polymer matrices; polypyrrole and poly(N-(4-(3-thienyl methylene)-oxycarbonyl phenyl) maleimide-co-pyrrole) via electrochemical method. Fourier transform infrared and scanning electron microscope were employed to characterize the copolymer of (N-(4-(3-thienyl methylene)-oxycarbonyl phenyl) maleimide) with pyrrole. Kinetic parameters, maximum reaction rate and Michealis-Menten constant, were determined. Effects of temperature and pH were examined for immobilized enzymes. Also, storage and operational stabilities of enzyme electrodes were investigated. Glucose and polyphenol oxidase enzyme electrodes were used for determination of the glucose amount in orange juices and human serum and phenolic amount in red wines, respectively.

Immobilization of invertase in conducting copolymers of 3-methylthienyl methacrylate.

Immobilization of invertase in conducting copolymer matrices of 3-methylthienyl methacrylate with pyrrole and thiophene was achieved by constant potential electrolysis using sodium dodecyl sulfate (SDS) as the supporting electrolyte. Polythiophene (PTh) was also used in entrapment process for comparison. Kinetic parameters, Michaelis-Menten constant, K(m), and the maximum reaction rate, V(max), were investigated. Operational stability and temperature optimization of the enzyme electrodes were also examined.

Immobilization of glucose oxidase in polypyrrole/polytetrahydrofuran graft copolymers.

Glucose oxidase (GOD) was immobilized in four different conducting polymer matrices, namely: polypyrrole, (PPy), poly(pyrrole-graft-polytetrahydrofuran), (1) and (3); and poly(pyrrole-graft-polystyrene/polytetrahydrofuran), (2). The kinetic parameters V(max) and K(m), and the optimum temperature were determined for both immobilized and native enzymes. The effect of electrolysis time and several supporting electrolytes, p-toluenesulfonic acid, p-toluene sulfonic acid (PTSA), sodium p-toluene sulfonate, sodium p-toluene sulfonate (NaPTS), and sodium dodecyl sulfate, sodium dodecyl sulfate (SDS), on enzyme immobilization were investigated. The high K(m) value (59.9 mM) of enzyme immobilized in PPy was decreased via immobilization in graft copolymer matrices of pyrrole. V(max), which was 2.25 mM/min for pure PPy, was found as 4.71 mM/min for compound (3).

Immobilization of invertase in conducting thiophene-capped poly(methylmethacrylate)/polypyrrole matrices.

Immobilization of invertase in thiophene-capped poly(methylmethacrylate)/polypyrrole matrices was achieved by constant potential electrolysis using different supporting electrolytes. Optimum reaction conditions such as substrate concentration, temperature, and pH for the enzyme electrodes were determined. The temperature and pH were found to be 60 degrees C and 4.8, respectively. The effect of supporting electrolyte on the enzyme activity revealed that SDS was the best in the immobilization procedure. Michaelis-Menten constant and the maximum reaction rate in PMMA/PPy matrices were of the order of that of pristine polypyrrole. However, in terms of repeated use, the copolymer matrices were superior to polypyrrole.