RESUMEN
In this work, synthesis, characterization and oxygen sensing abilities of the cyclophosphazene-free and phenyl and naphtoxy-substituted cyclophosphazene bearing iridium (III) complexes (Ir-I, Ir-II and Ir-III) were presented. The complexes were characterized by NMR, absorption and emission spectroscopies, luminescence lifetime and quantum yield measurements. The molecules were successfully embedded in the ethyl cellulose matrix to fabricate the oxygen sensing electrospun mats via electrospinning technique. Oxygen induced luminescence of the iridium complexes around 600 nm has been followed as the analytical signal during oxygen sensitivity studies. They exhibited blue shifted, quenched emission towards triplet oxygen. The napthoxy substituted derivative exhibited 2.70 fold enhanced I0/I100 ratio compared to the free form in terms of the relative signal change. Room-temperature luminescence abilities, high photostabilities, large Stoke's shift values extending to 200 nm and high spectral response, especially between 0 and 10% pO2 make them promising candidates as oxygen probes. The test materials can be stored at the ambient air of the laboratory for at least 24 months.
RESUMEN
In this presented study, a novel molecularly imprinted polymeric hydrogel membranes (PHMs) were developed to use for the albumin depletion studies. For this, albumin imprinted poly(2-hydroxyethyl methacrylate-N-methacryloyl-(L)-phenylalanine methyl ester) polymeric hydrogel membranes [p(HEMA-MAP) PHMs] were synthesized by the photopolymerization technique, and then characterized by SEM, EDX, FT-IR and swelling studies. Synthesized PHMs had spherical structure and the MAP monomer incorporation onto the PHMs was determined by EDX analysis by using nitrogen stoichiometry. Also, the swelling ratio of the albumin imprinted p(HEMA-MAP) PHMs was determined as 215%. The optimum albumin adsorption condition (adsorption capacity, medium pH, adsorption rate, temperature, ionic strength) were studied and the maximum albumin adsorption capacity was found to be as 34.28 mg/g PHMs. Selectivity experiments were also carried out with the presence of the competitive proteins such as lysozyme and amylase, and the results demonstrated that the albumin imprinted p(HEMA-MAP) PHMs showed high affinity towards the BSA molecules than the competitive proteins of lysozyme and amylase. Adsorbed albumin was desorbed from the PHMs by 1.0 M of NaCl, and the reusability of the imprinted PHMs was also demonstrated for five successive adsorption-desorption cycles without any significant loss in the albumin adsorption capacity. As an application, sodium-dodecyl sulfate polyacrylamide gel electrophoresis was used to indicate the albumin depletion efficiency of albumin imprinted p(HEMA-MAP) PHMs. This presented study showed that, these imprinted membranes are promising for proteomic studies and applications, and can be used for the investigations for human diagnostics.