P.G. Department of Studies in Chemistry, Karnatak University, Dharwad 580003, India.
Biopharm Drug Dispos. 2010 Mar;31(2-3):120-8. doi: 10.1002/bdd.696.
The binding of sulfacetamide sodium (SAS) to bovine serum albumin (BSA) was investigated by spectroscopic methods, namely fluorescence, FT-IR and UV-vis absorption spectral studies. The binding parameters were evaluated by a fluorescence quenching method. The thermodynamic parameters, DeltaH(0), DeltaS(0)and DeltaG(0) were observed to be -49.03 k J mol(-1), -99.9 J K(-1) mol(-1) and -18.96 k J mol(-1), respectively. These indicated that the hydrogen bonding and weak van der Waals forces played major roles in the interaction. Based on Förster's theory of non-radiation energy transfer, the binding average distance, r, between the donor (BSA) and acceptor (SAS) was evaluated and found to be 3.72 nm. The spectral results showed that binding of SAS to BSA induced conformational changes in BSA. The effect of common ions and some of the polymers used in drug delivery for controlled release were also tested on the binding of SAS to BSA.
采用荧光光谱、FT-IR 和紫外可见吸收光谱等光谱方法研究了磺胺醋酰钠（SAS）与牛血清白蛋白（BSA）的结合。通过荧光猝灭法评估了结合参数。观察到热力学参数ΔH(0)、ΔS(0)和ΔG(0)分别为-49.03 kJ/mol、-99.9 J K(-1)mol(-1)和-18.96 kJ/mol。这表明氢键和弱范德华力在相互作用中起主要作用。基于福斯特非辐射能量转移理论，评估了供体（BSA）和受体（SAS）之间的结合平均距离 r，发现为 3.72nm。光谱结果表明，SAS 与 BSA 的结合诱导了 BSA 的构象变化。还测试了常用离子和一些用于药物控释的聚合物对 SAS 与 BSA 结合的影响。
