Quantitation, Visualization, and Monitoring of Conformational Transitions of Human Serum Albumin by a Tetraphenylethene Derivative with Aggregation-Induced Emission Characteristics
Quantitation, Visualization, and Monitoring of Conformational Transitions of Human Serum Albumin by a Tetraphenylethene Derivative with Aggregation-Induced Emission Characteristics
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DOI：
10.1021/ac1018028
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发表时间：
2010-08-15
影响因子：
7.4
通讯作者：
Tang, Ben Zhong
中科院分区：
文献类型：
--
作者：
Hong, Yuning;Feng, Chao;Tang, Ben Zhong
人血清白蛋白（HSA）是血浆中的主要蛋白成分，其含量测定在生物学研究中具有重要价值。我们，在此，提出了一种易于获得的荧光生物探针的HSA检测和定量。一种不发光的四苯乙烯衍生物1，2-双[4-（3-磺酸丙氧基）苯基]-1，2-二苯基乙烯钠（BSPOTPE）被吲哚丁酸（IBA）诱导发光，表现出聚集诱导发光（AIE）现象。AIE生物探针具有宽的工作范围（0-100 nM）、低检测限（低至1 nM）和对白蛋白的上级选择性。荧光生物测定不受人工尿液中各种生物电解质的干扰。AIE发光团也可用作凝胶电泳中用于HSA可视化的快速和灵敏的蛋白质染色剂。利用BSPOTPE的AIE特性和HSA向BSPOTPE的Forster共振能量转移，对盐酸胍诱导的HSA去折叠过程进行了监测，揭示了一个包含熔融小球中间体的多步转变过程.计算模型表明，AIE发光体停靠在HSA的亚结构域IIA和IIIA之间的疏水裂缝的疏水效应，电荷中和和氢键相互作用的帮助下，提供了对疏水腔内部的微环境的机理洞察。
Human scrum albumin (HSA) is a major protein component of blood plasma, and its assay is of obvious value to biological research. We, herein, present a readily accessible fluorescent bioprobe for HSA detection and quantitation. A nonemissive tetraphenylethene derivative named sodium 1,2-bis[4-(3-sulfonatopropoxyl)phenyl]-1,2-diphenylethene (BSPOTPE) is induced to emit by IBA, showing a novel phenomenon of aggregation-induced emission (AIE). The AIE bioprobe enjoys a broad working range (0-100 nM), a low detection limit (down to 1 nM), and a superior selectivity to albumins. The fluorescent bioassay is unperturbed by the miscellaneous bioelectrolytes in the artificial urine. The AIE luminogen can also be used as a rapid and sensitive protein stain in gel electrophoresis for HSA visualization. Utilizing the AIE feature of BSPOTPE and the Forster resonance energy transfer from HSA to BSPOTPE, the unfolding process of HSA induced by guanidine hydrochloride is monitored, which reveals a multistep transition with the involvement of molten globule intermediates. Computational modeling suggests that the AIE luminogens dock in the hydrophobic cleft between subdomains IIA and IIIA of HSA with the aid of hydrophobic effect, charge neutralization, and hydrogen bonding interactions, offering mechanistic insight into the microenvironment inside the hydrophobic cavity.