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Dinuclear copper(II) complexes bridged with acetate and nitrate anions: Study of protein binding and in-vitro anticancer activity
[Display omitted] •Dinuclear copper complexes containing N-(3-pyridyl)-1,8-naphthalimide ligand has been synthesized.•Complexes have distorted square planar geometry around copper center.•Four acetate ions and two nitrate ions bridges the two copper center in complex 1 and complex 2 respectively.•BS...
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Published in: | Inorganica Chimica Acta 2024-01, Vol.559, p.121799, Article 121799 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites |
Online Access: | Get full text |
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Summary: | [Display omitted]
•Dinuclear copper complexes containing N-(3-pyridyl)-1,8-naphthalimide ligand has been synthesized.•Complexes have distorted square planar geometry around copper center.•Four acetate ions and two nitrate ions bridges the two copper center in complex 1 and complex 2 respectively.•BSA binding of complexes follow dynamic quenching mechanism.•Anticancer activity of the complexes has been studied using an MTT assay.
Two dinuclear copper(Ⅱ) complexes [Cu(L)(μ-AcO)2]2·H2O (1) and [Cu(L)(bpy)(μ-NO3)]2. (ClO4)2 (2) were synthesized with the ligand L = N-(3-pyridyl)-1,8-naphthalimide (where, OAc = Acetate, bpy = 2,2′-bipyridine). The complexes were characterized with FT-IR, UV–vis, fluorescence, EPR, and single crystal X-ray diffraction technique. Complex 1 contains two copper(Ⅱ) units bridged by four acetate ions via oxygen atoms having distorted square pyramidal geometry around both the copper(Ⅱ) centers. Complex 2 consists of two copper(Ⅱ) centers with two bridging nitrates via oxygen atoms in a distorted square pyramidal environment. The complexes 1 and 2 efficiently bind to BSA (bovine serum albumin) showing a dynamic quenching mechanism. The in-vitro anticancer activity have been investigated against HeLa cell lines using MTT assay. Complex 1 is two times more active than cisplatin under the same experimental conditions, whereas complex 2 is twelve times more active. |
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ISSN: | 0020-1693 1873-3255 |
DOI: | 10.1016/j.ica.2023.121799 |