Mandal Ujjwal, Ghosh Subhadip, Mitra Gopa, Adhikari Aniruddha, Dey Shantanu, Bhattacharyya Kankan
Physical Chemistry Department, Indian Association for the Cultivation of Science, Jadavpur, Kolkata, India.
Chem Asian J. 2008 Sep 1;3(8-9):1430-4. doi: 10.1002/asia.200800114.
The interaction of a protein, human serum albumin (HSA) with a surfactant (sodium dodecyl sulfate, SDS) was studied by femtosecond up-conversion. HSA was labeled covalently with a probe (CPM, 7-dimethylamino-3-(4-maleimidophenyl)-4-methylcoumarin). Binding of SDS to HSA is found to accelerate the solvation dynamics approximately 1.3-fold. The solvation dynamics in HSA displays two time components: 30 ps (20 %) and 800 ps (80 %). When approximately 10 SDS molecules bind to HSA the components are 15 ps (40 %) and 800 ps (60 %). It is argued that SDS may increase the solvent exposure of the probe (CPM); it may also displace the buried water molecules in the immediate vicinity of CPM.
通过飞秒上转换技术研究了蛋白质人血清白蛋白（HSA）与表面活性剂十二烷基硫酸钠（SDS）之间的相互作用。HSA用探针（CPM，7-二甲基氨基-3-（4-马来酰亚胺基苯基）-4-甲基香豆素）进行共价标记。发现SDS与HSA的结合使溶剂化动力学加速了约1.3倍。HSA中的溶剂化动力学表现出两个时间成分：30皮秒（20%）和800皮秒（80%）。当约10个SDS分子与HSA结合时，成分变为15皮秒（40%）和800皮秒（60%）。有人认为，SDS可能会增加探针（CPM）的溶剂暴露；它也可能取代CPM紧邻区域中埋藏的水分子。
