Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 4 de 4
Filtrar
Más filtros











Base de datos
Intervalo de año de publicación
1.
Artículo en Inglés | MEDLINE | ID: mdl-25025307

RESUMEN

The sonodynamic damage to protein in the presence of methylene blue (MB) and the various influencing factors including ultrasonic irradiation time and MB concentration on the damage of protein were studied by fluorescence and absorption spectra. In addition, the mechanisms of the synergistic effects of ultrasound and MB were studied by oxidation-extraction photometry with several reactive oxygen species (ROS) scavengers. The results indicated that the damage of protein induced by the synergistic effects of ultrasound and MB were more serious than those that ultrasound or MB alone was applied. The damage of protein could be mainly due to the generation of ROS. The damage degree of protein increased with the increase of ultrasonic irradiation time and MB concentration because of the increased quantities of ROS generation. Both (1)O2 and ·OH were the important mediators of the ultrasound-inducing protein damage in the presence of MB.


Asunto(s)
Azul de Metileno/efectos adversos , Especies Reactivas de Oxígeno/química , Albúmina Sérica Bovina/química , Sonicación/efectos adversos , Animales , Bovinos , Espectrometría de Fluorescencia , Ultrasonido
2.
Iran J Pharm Res ; 13(4): 1183-90, 2014.
Artículo en Inglés | MEDLINE | ID: mdl-25587306

RESUMEN

Three new rimantadine Schiff bases (RSBs) were prepared, and then the interaction of RSBs with bovine serum albumin (BSA) was investigated using fluorescence, synchronous fluorescence, UV-vis absorption spectroscopy under physiological conditions. The results showed that the three RSBs effectively quenched the intrinsic fluorescence of BSA via static quenching. Binding constant (K a), number of binding sites (n), and the binding distance (r) between three RSBs and BSA were calculated by Stern-Volmer equation and Förster's theory in this study. According to the results of displacement experiments of site probes, it was considered that the binding sites were located in hydrophobic cavities in sub-domains IIA of BSA. What is more, synchronous fluorescence studies indicated that the hydrophobicity around tryptophan residues was increased with the addition of rimantadine-o-vanillin (ROV) and rimantadine-4-methoxy-salicylaldehyde (RMS), while there was no apparent change with the addition of rimantadine-salicylaldehyde (RS).

3.
Artículo en Inglés | MEDLINE | ID: mdl-21177138

RESUMEN

In recent years, sonodynamic activities of many drugs have attracted more and more attention of researchers. The correlative study will promote the development of sonodynamic therapy (SDT) in anti-tumor treatment. In this work, bovine serum albumin (BSA) was used as a protein model to investigate the intensifying effects of ciprofloxacin (CPFX) ultrasonically induced protein damage by UV-vis and fluorescence spectra. Meanwhile, the conformation of BSA is changed upon the addition of CPFX and metal ions under ultrasound (US) so that the damaging site of BSA is considered. Various influencing factors, such as US irradiation time, metal ions, solution temperature and ionic strength, on the ultrasonically induced BSA damage are discussed. It was showed that CPFX could enhance ultrasonically induced BSA damage. The damage degree of BSA was aggravated with the increasing of US irradiation time, solution temperature, ionic strength as well as the addition of metal ions. Furthermore, the reactive oxygen species (ROS) in reaction system were detected by oxidation-extraction photometry (OEP). Experimental results also showed that US could activate CPFX to produce ROS, which were mainly determined as superoxide radical anion (.O2-) and hydroxyl radical (.OH).


Asunto(s)
Ciprofloxacina/farmacología , Albúmina Sérica Bovina/efectos de los fármacos , Albúmina Sérica Bovina/efectos de la radiación , Ultrasonido/métodos , Absorción/efectos de los fármacos , Absorción/efectos de la radiación , Animales , Bovinos , Ciprofloxacina/química , Metales , Concentración Osmolar , Conformación Proteica/efectos de los fármacos , Conformación Proteica/efectos de la radiación , Especies Reactivas de Oxígeno/química , Albúmina Sérica Bovina/química , Soluciones , Espectrometría de Fluorescencia , Espectrofotometría Ultravioleta , Temperatura , Factores de Tiempo , Ultrasonido/instrumentación , Xantenos/química
4.
J Fluoresc ; 20(5): 985-92, 2010 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-20358282

RESUMEN

Taking bovine serum albumin (BSA) as typical molecules, the sonodynamic damage of protein in the presence of Levofloxacin (LVFX) and its mechanism were studied by fluorescence and UV-vis spectra. Various influencing factors such as ultrasonic irradiation time, pH value, ionic strength and solution temperature on the damage of BSA were also discussed. The results showed that ultrasound can enhance the damage of LVFX on BSA. The damage degree of BSA was aggravated with the increase of ultrasonic irradiation time, solution temperature and ionic strength, whereas decreased with the increase of solution pH value. Furthermore, the reactive oxygen species (ROS) in reaction system were studied by oxidation and extraction photometry. Experimental results showed that the amounts of superoxide anion radical (·O(2)(-)) and hydroxyl radical (·OH) were significantly more than that of singlet oxygen ((1)O(2)) in the presence of LVFX under ultrasonic irradiation.


Asunto(s)
Levofloxacino , Ofloxacino/química , Albúmina Sérica Bovina/química , Análisis Espectral/métodos , Animales , Bovinos , Fluorescencia , Concentración de Iones de Hidrógeno , Radical Hidroxilo , Concentración Osmolar , Oxidación-Reducción , Especies Reactivas de Oxígeno/análisis , Espectrometría de Fluorescencia , Espectrofotometría Ultravioleta , Superóxidos , Temperatura , Ultrasonido
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA