Journal
POLYHEDRON
Volume 157, Issue -, Pages 39-48Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.poly.2018.09.023
Keywords
Double mu(2)-(phenoxido)-bridged; Ni(II) complex; Crystal structure; Magnetic properties; DNA/protein binding
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Funding
- Government of India [01 (2743)/13/EMR-II]
- Spanish Ministerio de Economia y Competitividad (MINECO) [CTQ2012-32247, RYC-2010-05821]
- regional Generalitat de Catalunya authority [2014SGR-129]
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One dinuclear and one 1D polymeric nickel(II) complex, namely {[Ni-2(HL)(2)(pa)(2)(H2O)(2)]center dot DME} (1) and {[Ni-2(HL)(2)(ppda)(2)(H2O)(2)]center dot DME center dot H2O}(n )(2) (H2L = (E)-2-((1-hydroxybutan-2-ylimino)methyl)phenol, pa = 3-phenylacrylate, ppda =p-phenylenediacrylate) have been synthesized and characterized by X-ray single crystal structure determination. Complex 1 is double phenoxo-bridged dinuclear Ni(II) complex, whereas complex 2 is a 1D polynuclear chain where double phenoxo-bridged dinuclear units are connected through bridging ppda ligands. The variable temperature magnetic behavior of the complexes was studied using the Hamiltonian H = JS(1)S(2), S-1 = S-2 = S-Ni and confirms the presence of an overall anti-ferromagnetic interaction in both complexes. Good agreement between the experimental and simulated curves were found using the parameters: g(Ni)= 2.15, D-Ni = 4.0 cm(-1 )and J(Ni-Ni )= -0.60 cm(-1) for 1, and g(Ni)= 2.15, D-Ni = 4.8 cm(-1) and J(Ni-Ni) = -3 cm(-1) for 2. The interactions of the complexes with CT-DNA were investigated using UV-Vis absorption and fluorescence spectroscopic methods and they show that both the complexes interact with CT-DNA. The intrinsic binding constants values for interaction with CT-DNA are 3.9(+/- 0.10) x 10(5) and 3.43(+/- 0.09) x 10(5)M(-1) for 1 and 2, respectively. The interactions of the complexes with bovine serum albumins (BSA) and human serum albumins (HSA) were also studied using electronic absorption and fluorescence spectroscopic techniques and the results show that both complexes interact with the serum albumins via a ground state association process. (C) 2018 Elsevier Ltd. All rights reserved.
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