金属离子诱导人中心蛋白3的聚集  

Metal Ions-induced Aggregation of Human Centrin 3

作　　者：赵亚琴[1] 王映杰 ZHAO Yaqin;WANG Yingjie(Institute of Molecular Science,Shanxi University,Taiyuan 030006,China)

机构地区：[1]山西大学分子科学研究所,山西太原030006

出　　处：《山西大学学报（自然科学版）》2022年第5期1342-1349,共8页Journal of Shanxi University(Natural Science Edition)

基　　金：国家自然科学基金(20901048,21571117);教育部博士点专项基金(20131401110011)。

摘　　要：人中心蛋白3(Human centrin 3,HsCen3)是一种分子量比较小(约20 kD)的酸性、钙离子结合蛋白。在0.01 mol/L Hepes(N-2-Hydroxyethylpiperazine-N-2-ethanesulfonic acid)、pH 7.4和25℃条件下,本文通过荧光共振光散射方法研究了稀土离子(La^(3+)nthanide,Ln^(3+))、Ca^(2+)诱导HsCen3聚集的热力学性质及离子强度、离子半径等因素对蛋白聚集的影响。结果表明Ln^(3+)、Ca^(2+)都可以诱导HsCen3形成聚集体,Ln^(3+)对HsCen3的聚集效应明显强于Ca^(2+);在HsCen3形成聚集体过程中,其N-端结构域起主要作用、C-端结构域起次要作用;随着稀土离子半径减小,从La^(3+)到Lu^(3+)对HsCen3的聚集效应逐渐增强;疏水探针占据HsCen3蛋白疏水结构域后蛋白聚集程度减小,推测静电作用力以及疏水作用是促使HsCen3发生聚集的主要驱动力。Human centrin 3 (HsCen3) is a kind of acidic calcium binding protein with relatively small molecular weight (about 20kD).The thermodynamics of La^(3+)nthanide (Ln^(3+)) and Ca^(2+)-induced HsCen3 aggregation,as well as the effects of ionic strength and ionic radius on protein aggregation were studied by fluorescence resonance light scattering,in the 0.01 mol/L Hepes (N-2-Hydroxyethylpiperazine-N-2-ethanesulfonic acid) at p H 7.4 and 25℃.The results indicated that Ln^(3+)and Ca^(2+)could induce HsCen3 to form dimer,trimer,tetramer or oligomer.The effects of Ln^(3+)on HsCen3 aggregation were obviously higher than that of Ca^(2+).The N-terminal domain plays major role in the formation of HsCen3 aggregates,while the C-terminal domain plays secondary role.With the increasing ion radius of Ln^(3+),HsCen3 aggregation became stronger.When the hydrophobic probe occupied the hydrophobic domain of HsCen3 protein,the degree of HsCen3 aggregation decreased.It is speculated that electrostatic force and hydrophobic interaction are the main driving forces for HsCen3 aggregation.

关 键 词：人中心蛋白3 聚集 荧光共振光散射 

分 类 号：O641.4[理学—物理化学]