PubMed · 16196227
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John L Guinta. 2005. 'A simpler technique'.. https://doi.org/10.14219/jada.archive.2005.0330
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Nanotubes of poly(4-vinylpyridine) (PVP) and poly(acrylic acid) (PAA) were fabricated by hydrogen bonding based on layer-by-layer (LbL) assembly. The uniform and flexible tubular structures were characterized by scanning electron microscopy (SEM) and transmission electron microscopy (TEM). FTIR and X-ray photoelectron spectroscopy (XPS) measurements confirm the formation of hydrogen bonds in the assembled nanotubes. PAA can be released from the assembled PAA/PVP nanotubes in a basic aqueous solution to give the walls of the tubes a porous structure. Such assembled nanotubes can be considered as carriers for catalysts or drugs, especially in aqueous solution against capillary force.
Polymeric coatings with high protein-binding capacities are important for increasing the output of affinity-based protein purification and decreasing the detection limits of antibody microarrays. This report describes the use of thick poly(acrylic acid) (PAA) brushes to immobilize as much as 80 monolayers of protein. The brushes were prepared using a recently developed procedure that allows polymerization of 100-nm-thick poly(tert-butyl acrylate) films from a surface in just 5 min along with hydrolysis of these films to PAA in 15 min. Covalent binding of bovine serum albumin (BSA) to PAA brushes that were activated using standard coupling agents, however, resulted in immobilization of less than two monolayers of BSA because of competitive hydrolysis of the esters in the activated film. In contrast, derivatization of PAA with nitrilotriacetate (NTA)-Cu2+ complexes yielded films capable of binding many monolayers of protein via metal-ion affinity interactions. For example, derivatization of 55-nm-thick PAA films with NTA-Cu2+ allowed immobilization of about 15 monolayers (5.8 microg/cm2 or 58 nm) of BSA. The binding capacity was even higher for myoglobin (7.7 microg/cm2) and anti-IgG (9.6 microg/cm2). Remarkably, electrostatic adsorption of lysozyme in 55-nm-thick, underivatized PAA resulted in as much as 80 monolayers (16.2 microg/cm2 or 162 nm) of adsorbed protein. Polymer synthesis, derivatization, and swelling, as well as BSA immobilization kinetics and thermodynamics were characterized using reflectance FT-IR spectroscopy, ellipsometry, and protein assays.
OBJECTIVES: This study compared the residual monomer (RM) in four hard chair-side reline resins (Duraliner II-D, Kooliner-K, Tokuso Rebase Fast-TRF and Ufi Gel hard-UGH) and one heat-polymerized denture base resin (Lucitone 550-L), which was processed using two polymerization cycles (short-LS and long-LL). It was also investigated the effect of two after polymerization treatments on this RM content. METHODS: Specimens (n=18) of each material were produced following the manufacturers' instructions and then divided into three groups. Group I specimens were left untreated (GI-control). Specimens of group II (GII) were given post-polymerization treatment by microwave irradiation. In group III (GIII), specimens were submitted to immersion in water at 55 degrees C (reline resins-10 min; denture base resin L-60 min). The RM was analyzed using high performance liquid chromatography (HPLC) and expressed as a percentage of RM. Data were analyzed by two-way ANOVA followed by Tukey's test (alpha=0.05). RESULTS: Comparing control specimens, statistical differences were found among all materials (p<0.05), and the results can be arranged as K (1.52%)>D (0.85%)>UGH (0.45%)>LL (0.24%)>TRF (0.14%)>LS (0.08%). Immersion in hot water (GIII) promoted a significant (p<0.05) reduction in the RM for all materials evaluated compared to control (GI), with the exception of LL specimens. Materials K, UGH and TRF exhibited significantly (p<0.05) lower values of RM after microwave irradiation (GII) than in the control specimens. SIGNIFICANCE: The reduction in RM promoted by water-bath and microwave post-polymerization treatments could improve the mechanical properties and biocompatibility of the relining and denture base materials.