School of Chemistry, Bharathidasan University, Tiruchirappalli 620024, Tamil Nadu, India.
J Hazard Mater. 2010 Mar 15;175(1-3):985-91. doi: 10.1016/j.jhazmat.2009.10.107. Epub 2009 Oct 30.
The interaction between lysozyme and anthraquinone dyes such as Alizarin Red S, Acid blue 129 and Uniblue was studied using steady state, time resolved fluorescence measurements and docking studies. Addition of anthraquinone dyes effectively quenched the intrinsic fluorescence of lysozyme. Fluorescence quenching of lysozyme by dyes has revealed the formation of complex. The number of binding sites (n) and binding constant (K) for all the three dyes was calculated by relevant fluorescence quenching data. Based on Förster's non-radiative energy transfer theory, distance (r(0)) between the donor (lysozyme) and acceptor (dyes) as well as the critical energy transfer distance (R(0)) has also been calculated. The interaction between dyes and lysozyme occurs through static quenching mechanism as confirmed by time resolved spectroscopy. The conformational change of lysozyme has been analyzed using synchronous fluorescence measurement. Finally, docking studies revealed that specific interactions were observed with the residue of Trp 62.
采用稳态、时间分辨荧光测量和对接研究研究了溶菌酶与茜素红 S、酸性蓝 129 和 Uniblue 等蒽醌染料之间的相互作用。蒽醌染料的添加有效地猝灭了溶菌酶的固有荧光。染料对溶菌酶的荧光猝灭揭示了复合物的形成。通过相关的荧光猝灭数据计算了所有三种染料的结合位点数 (n) 和结合常数 (K)。根据福斯特非辐射能量转移理论，还计算了供体 (溶菌酶) 和受体 (染料) 之间的距离 (r(0)) 以及临界能量转移距离 (R(0))。时间分辨光谱证实染料与溶菌酶之间的相互作用通过静态猝灭机制发生。使用同步荧光测量分析了溶菌酶的构象变化。最后，对接研究表明观察到与色氨酸残基 62 的特异性相互作用。
