کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5402775 1392741 2010 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Spectroscopic studies on the interaction and sonodynamic damage of neutral red (NR) to bovine serum albumin (BSA)
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
Spectroscopic studies on the interaction and sonodynamic damage of neutral red (NR) to bovine serum albumin (BSA)
چکیده انگلیسی
In this paper, the interaction of neutral red (NR) with bovine serum albumin (BSA) and the sonodynamic damage to BSA under ultrasonic irradiation was studied by means of ultraviolet-visible (UV-vis) and fluorescence spectra. The quenching constant (KSV=5.749×104 L/mol), binding constant (KA=3.19×104 L/mol) and binding site number (n=0.9462) were measured. The binding distance (r=2.47 nm) between NR and BSA was obtained according to Föster's non-radiative energy transfer theory. The damage process of BSA molecules was detected by the hyperchromic effect of UV-vis spectra and quenching of intrinsic fluorescence spectra. In addition, the influencing factors such as ultrasonic irradiation time and NR concentration on the damage to BSA molecules were also considered. The results showed that the damage degree is enhanced with the increase of ultrasonic irradiation time and NR concentration. The possible mechanism of sonodynamic damage to BSA molecules was mainly mediated by singlet oxygen (1O2). Otherwise, the binding and damaging sites to BSA molecules were also estimated by synchronous fluorescence. The results indicated that the NR is more vicinal to tryptophan (Trp) residue than to tyrosine (Tyr) residue and the damage site is also mainly at Trp residues. The research result will bring a certain significance to use sonosensitive drugs in the fields of tumor treatment.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Luminescence - Volume 130, Issue 6, June 2010, Pages 1036-1043
نویسندگان
, , , , , , , ,