摘要
采用亲和毛细管电泳法,研究了牛血清蛋白(BSA)与两种结构相似的羧酸类化合物肉桂酸(CA)和阿魏酸(FA)间的相互作用。采用淌度比计算得到25℃时CA与FA的结合常数分别为3.5318×104L/mol、8.0158×104L/mol,并根据不同温度的结合常数计算了ΔS、ΔH、ΔG等热力学参数。热力学参数表明,CA、FA与BSA体系间的相互作用力以氢键作用力和范德华作用力为主。
The interactions of bovine serum albumin（BSA） with cinnamic acid（CA） and ferulic acid（FA） were simultaneous studied by capillary electrophoresis（CE）.Mobility ratio was used to deduce the binding constant（Kb）.The Kb was 3.5318×104 L/mol and 8.0158×104 L/mol at 25 ℃ for CA and FA.The thermodynamic parameters were obtained from data at different temperatures,and the negative ΔH and positive ΔS values showed that both hydrogen bonds and van der Waals interactions played major roles in the binding of aromatic acids to BSA.
出处
《广州化工》
CAS
2012年第20期70-72,86,共4页
GuangZhou Chemical Industry
