首页|A muconate bridged bipyridyl appended binuclear Cu(II) complex reveals dissimilar affinities to DNA and BSA protein
A muconate bridged bipyridyl appended binuclear Cu(II) complex reveals dissimilar affinities to DNA and BSA protein
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NSTL
Elsevier
A new muconate based Cu(II) metal complex, [Cu-2(muco)(5,5'-Me(2)bpy)4].2ClO(4) butadiene-1,4-dicarboxylic acid or trans , trans-muconic acid and 5,5'-Me2bpy = 5,5'-dimethyl-2,2'-bipyridine), has been synthesized and structurally characterized. X-ray structure analysis reveals that 1 forms a binuclear complex with a five coordinated square pyramidal geometry of the central Cu(II) ion attached to a muco and two bipyridine ligands. Docking studies have been carried out which reveal the successful binding of the metal complex to the major groove of DNA and the planar aromatic bipyridyl ligand partially intercalates into the base pairs. The synthesized complex fits into the pocket of bovine serum albumin (BSA), while the maximum fraction submerges into the BSA binding pocket. An extra coordinate bond has been found, forming through the oxygen atom of 158 asparagines amino acid, which subsequently forms a new six coordinated octahedral complex. Experimental studies have been performed to validate all the data obtained from the docking studies. This study reveals highly diverse affinities and binding modes of the synthesized complex towards DNA and protein. Therefore, the synthesized complex may pave the way to be used as a specific protein binder (low affinity to DNA or RNA) bioactive compound.
NSTL
Elsevier
