烷氧基桥连双核铼（I）配合物作为β-淀粉样蛋白聚集的潜在传感器。
Alkoxy bridged binuclear rhenium (I) complexes as a potential sensor for β-amyloid aggregation.
作者信息
Sathish Veerasamy, Babu Eththilu, Ramdass Arumugam, Lu Zong-Zhan, Velayudham Murugesan, Thanasekaran Pounraj, Lu Kuang-Lieh, Rajagopal Seenivasan
机构信息
School of Chemistry, Madurai Kamaraj University, Madurai 625 021, India; Department of Chemistry, Bannari Amman Institute of Technology, Sathyamangalam, India.
School of Chemistry, Madurai Kamaraj University, Madurai 625 021, India; Department of Chemistry, V.V. College of Engineering, Tisayanvilai, Tirunelveli, India.
出版信息
Talanta. 2014 Dec;130:274-9. doi: 10.1016/j.talanta.2014.06.070. Epub 2014 Jul 7.
Alkoxy bridged binuclear rhenium(I) complexes are used as a probe for the selective and sensitive detection of aggregation of β-amyloid fibrils that are consorted with Alzheimer's disease (AD). The strong binding of the complexes is affirmed by the fluorescence enhancement and calculated binding constant value in the order of 10(5)M(-1) is obtained from the Scatchard plots. The binding of β-amyloid can be attributed to π-π stacking interaction of naphthalene moiety present in rhenium(I) complexes, and it is supported by docking studies. The selectivity is quite high towards other proteins and the formation of fibrils can be observed in the range of 30-40 nm through the AFM and TEM techniques.
烷氧基桥联双核铼（I）配合物被用作一种探针，用于选择性和灵敏地检测与阿尔茨海默病（AD）相关的β-淀粉样蛋白原纤维的聚集。配合物的强结合通过荧光增强得到证实，并且从Scatchard图获得了约10⁵M⁻¹的计算结合常数。β-淀粉样蛋白的结合可归因于铼（I）配合物中萘部分的π-π堆积相互作用，对接研究也支持了这一点。对其他蛋白质的选择性相当高，并且通过原子力显微镜（AFM）和透射电子显微镜（TEM）技术可以在30 - 40纳米范围内观察到原纤维的形成。
Zotero 插件