DNA/protein binding and magnetic properties of a 1D Cu(II) complex containing fumarate and tridentate Schiff base ligands
ID copper(II) complex, [Cu2(L)2(fum)]∙H2O}n (1) has been synthesized using fumarate (fum2-) and a Schiff base (HL), derived from the condensation reaction of 2-amino-1-butanol and salicyldehyde. Complex 1 has been characterized by X-ray crystal structure, FT-IR, electronic absorption and fluorescenc...
| Authors: | , , , |
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| Format: | article |
| Status: | Versión aceptada para publicación |
| Publication Date: | 2016 |
| Country: | España |
| Institution: | Universidad de Barcelona |
| Repository: | Dipòsit Digital de la UB |
| OAI Identifier: | oai:diposit.ub.edu:2445/154910 |
| Online Access: | https://hdl.handle.net/2445/154910 |
| Access Level: | Open access |
| Keyword: | ADN Estructura cristal·lina (Sòlids) Propietats magnètiques Lligands DNA Layer structure (Solids) Magnetic properties Ligands |
| Summary: | ID copper(II) complex, [Cu2(L)2(fum)]∙H2O}n (1) has been synthesized using fumarate (fum2-) and a Schiff base (HL), derived from the condensation reaction of 2-amino-1-butanol and salicyldehyde. Complex 1 has been characterized by X-ray crystal structure, FT-IR, electronic absorption and fluorescence spectroscopic methods. The structural determination reveals that complex 1 crystallizes in the monoclinic system with space group P21/n and form 1D polymeric chain, built by bridging fum. Weak π¿π and C-H¿π interactions in 1, lead to a 3D supramolecular architecture. Complex 1 exhibits fluorescence at room temperature with a quantum yield (Φs) of 0.257. The interactions of complex 1 with bovine serum albumin (BSA) and human serum albumin (HSA) were studied using electronic absorption and fluorescence spectroscopic techniques and the analysis shows that complex 1 interaction with BSA / HSA occurs mainly with ground state association process. Calculated values of apparent association constants are 1.34 × 104 M-1 and 1.81 × 104 M-1 for BSA and HAS, respectively, at 300 K. The number of binding sites and binding constants were calculated using double logarithm regression equation. The interaction of complex 1 with the calf thymus DNA (CT-DNA) was also investigated using electronic absorption and fluorescence spectroscopic methods. The results show that complex 1 has binding affinity to CT-DNA in the order of 2.96×105 M-1. Low temperature magnetic measurements reveal existence of antiferromagnetic interaction in complex 1. The magnetic data have been fitted considering complex 1 as a pseudo-dinuclear system, with the two copper(II) atoms bridged by two carboxylate oxygen atoms, since the coupling through long fum bridge is almost nil. The best-fit parameters obtained with this model are J = - 60 cm-1, gCu = 2.20. |
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