A chiral binuclear nickel(II) complex with Schiff base ligand: synthesis, crystal structure, DNA/BSA binding interaction
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A chiral binuclear nickel(II) complex with Schiff base ligand: synthesis, crystal structure, DNA/BSA binding interactions and SOD activity Jianfang Dong1,2 · Lei Gao3 · Peiran Zhao3 · Bo Zhang1 · Lei Wang1 · Jinming Kong4 · Lianzhi Li1 Received: 10 February 2020 / Accepted: 18 April 2020 © Springer Nature Switzerland AG 2020
Abstract A chiral binuclear Ni(II) complex [ Ni2(o-van-ala)2(phen)2] (o-van-ala = a Schiff base derived from o-vanillin and l-alanine, phen = 1,10-phenanthroline) has been synthesized and characterized by physicochemical and spectroscopic methods. Singlecrystal X-ray diffraction result showed that the Ni(II) complex contains two nickel centers, which are further bridged and coordinated by two o-van-ala Schiff base and two phen ligands in a cis-conformation. Each nickel atom is six-coordinated in a distorted NiN3O3 octahedral geometry. The interaction of the Ni(II) complex with calf thymus DNA (CT-DNA) has been investigated by spectroscopic methods. Based on results obtained, an intercalative binding mode has been proposed. In addition, the interaction between the Ni(II) complex and bovine serum albumin (BSA) has also been studied by various spectroscopic techniques. Results indicated that the Ni(II) complex can quench the intrinsic fluorescence of BSA in a static quenching process. The binding constant (Kb) and the number of binding sites (n) were calculated to be 2.92 × 106 M−1 and 1.21, respectively. Site-selective competitive binding experiment indicated that the binding site of the Ni(II) complex locates in site I in sub-domains IIA of BSA. The Ni(II) complex also displayed a significant superoxide anion scavenging activity.
Introduction Interactions between bio-macromolecules and drugs have attracted special interests of chemists and biologists. These bio-macromolecules, such as DNA, involving gene replication, transcription, mutation, are one of the main molecular Lei Gao: Co-first author. Electronic supplementary material The online version of this article (https://doi.org/10.1007/s11243-020-00390-z) contains supplementary material, which is available to authorized users. * Lianzhi Li [email protected] 1
School of Chemistry and Chemical Engineering, Liaocheng University, No. 1, Hunan Road, Liaocheng 252059, People’s Republic of China
2
Department of Material Science, Shandong Polytechnic Technician College, Liaocheng 252027, People’s Republic of China
3
Liaocheng People’s Hospital, Liaocheng 252000, People’s Republic of China
4
School of Environmental and Biological Engineering, Nanjing University of Science and Technology, 200 Xiaolingwei, Nanjing 210094, People’s Republic of China
targets of anticancer compounds. Proteins, particularly serum proteins, are of great interest because drugs can bind to them and affect the transportation and distribution of these drugs in human body [1]. Hence, to study the structures and properties of drugs, and interactions between drugs and proteins or DNA are highly required [2–6]. Since the discovery of cisplatin, extensiv
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