RESUMO
Gold nanoparticles can produce reactive oxygen species (ROS) under the action of ultrashort pulsed light. While beneficial for photodynamic therapy, this phenomenon is prohibitive for other biomedical applications such as imaging, photo-thermal drug release, or targeted gene delivery. Here, ROS are produced in water by irradiating gold nanorods and silica-coated gold nanorods with near-infrared femtosecond laser pulses and are detected using two fluorescent probes. Our results demonstrate that a dense silica shell around gold nanorods inhibits the formation of singlet oxygen (1O2) and hydroxyl radical (ËOH) efficiently. The silica coating prevents the Dexter energy transfer between the nanoparticles and 3O2, stopping thus the generation of 1O2. In addition, numerical simulations accounting for the use of ultrashort laser pulses show that the plasmonic field enhancement at the nanoparticle vicinity is lessened once adding the silica layer. With the multiphotonic ejection of electrons being also blocked, all the possible pathways for ROS production are hindered by adding the silica shell around gold nanorods, making them safer for a range of biomedical developments.
Assuntos
Materiais Revestidos Biocompatíveis/farmacologia , Ouro/farmacologia , Nanotubos/química , Fármacos Fotossensibilizantes/farmacologia , Espécies Reativas de Oxigênio/metabolismo , Dióxido de Silício/farmacologia , Materiais Revestidos Biocompatíveis/síntese química , Materiais Revestidos Biocompatíveis/química , Ouro/química , Humanos , Lasers , Teste de Materiais , Fármacos Fotossensibilizantes/síntese química , Fármacos Fotossensibilizantes/química , Dióxido de Silício/químicaRESUMO
In this paper we propose an easy way to detect the glycated form of human serum albumin which is biomarker for several diseases such as diabetes and Alzheimer. The detection platform is a label free impedimetric immunosensor, in which we used a monoclonal human serum albumin antibody as a bioreceptor and electrochemical impedance as a transducing method. The antibody was deposited onto a gold surface by simple physisorption technique. Bovine serum albumin was used as a blocking agent for non-specific binding interactions. Cyclic voltammetry and electrochemical impedance spectroscopy were used for the characterization of each layer. Human serum albumin was glycated at different levels with several concentrations of glucose ranging from 0â¯mM to 500â¯mM representing physiological, pathological (diabetic albumin) and suprapathological concentration of glucose. Through the calibration curves, we could clearly distinguish between two different areas related to physiological and pathological albumin glycation levels. The immunosensor displayed a linear range from 7.49% to 15.79% of glycated albumin to total albumin with a good sensitivity. Surface plasmon resonance imaging was also used to characterize the developed immunosensor.