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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 O 2 and OH were the important mediators of the ultrasound-inducing protein damage in the presence of MB. [ABSTRACT FROM AUTHOR]

Abstract: In this paper, the bovine serum albumin (BSA) was selected as a target molecule, the sonodynamic damage to protein in the presence of promethazine hydrochloride (PMT) and its mechanism were studied by the means of absorption, fluorescence and circular dichroism (CD) spectra. The results of hyperchromic effect of absorption spectra and quenching of intrinsic fluorescence spectra indicate that the ultrasound-induced BSA molecules damage is enhanced by PMT. The damage degree of BSA molecules increases with the increase of ultrasonic irradiation time and PMT concentration. The results of synchronous fluorescence, three-dimensional fluorescence and CD spectra confirmed that the synergistic effects of ultrasound and PMT induced the damage of BSA molecules. The results of oxidation–extraction photometry with several reactive oxygen species (ROS) scavengers indicate that the damage of BSA molecules could be mainly due to the generation of ROS and both 1O2 and e important mediators of the ultrasound-induced BSA molecules damage in the presence of PMT. [Copyright &y& Elsevier]

Abstract: The eight-coordinate (enH2)[YIII(pdta)(H2O)]2·10H2O (en=ethylenediamine and H4pdta=1,3-propylenediamine-N,N,N′,N′-tetraacetic acid) was synthesized, meanwhile its molecular and crystal structures were determined by single-crystal X-ray diffraction technology. The interaction between [YIII(pdta)(H2O)]2 2− and bovine serum albumin (BSA) was investigated by UV–vis and fluorescence spectra. The results indicate that [YIII(pdta)(H2O)]2 2− quenched effectively the intrinsic fluorescence of BSA via a static quenching process with the binding constant (K a) of the order of 104. Meanwhile, the binding and damaging sites to BSA molecules were also estimated by synchronous fluorescence. Results indicate that the hydrophobic environments around Trp and Tyr residues were all slightly changed. The thermodynamic parameters (ΔG =−25.20kJmol−1, ΔH= −26.57kJmol−1 and ΔS= −4.58Jmol−1 K−1) showed that the reaction was spontaneous and exothermic. What is more, both ΔH and ΔS were negative values indicated that hydrogen bond and Van der Waals forces were the predominant intermolecular forces between [YIII(pdta)(H2O)]2 2− and BSA. [ABSTRACT FROM AUTHOR]