Synthesis, crystal structure, optical and DFT studies of a novel Co(II) complex with the mixed ligands 3-bromothiophene-2-carboxylate and 2-aminopyridine

Muthukumar, M.; Karthikeyan, A.; Kamalesu, Subramaniam; Kadri, Mekki; Jennifer, Samson Jegan; Razak, Ibrahim Abdul; Nehru, Selvan

doi:10.1016/j.molstruc.2022.133953

Cited by 5 publications

(1 citation statement)

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“…This suggestion is also supported from the single crystal XRD data of the complex 2 and 5 , where the existence of this kind of coordination results in a paddle wheel structure. The attachment of the substituted pyridine moieties in the complexes is evident from the appearance of vibrational bands responsible for Cu-N bond around 500–550 cm −1 [ 25 ]. Furthermore, the vibrational band around 2200 cm −1 attributed to the stretching of the cyano group (C≡N) of 3-CNPy and 4-CNPy also confirms the presence of these moieties [ 26 ].…”

Section: Resultsmentioning

confidence: 99%

Synthesis, Structural Elucidation and Pharmacological Applications of Cu(II) Heteroleptic Carboxylates

et al. 2023

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Six heteroleptic Cu(II) carboxylates (1–6) were prepared by reacting 2-chlorophenyl acetic acid (L1), 3-chlorophenyl acetic acid (L2), and substituted pyridine (2-cyanopyridine and 2-chlorocyanopyridine). The solid-state behavior of the complexes was described via vibrational spectroscopy (FT-IR), which revealed that the carboxylate moieties adopted different coordination modes around the Cu(II) center. A paddlewheel dinuclear structure with distorted square pyramidal geometry was elucidated from the crystal data for complexes 2 and 5 with substituted pyridine moieties at the axial positions. The presence of irreversible metal-centered oxidation reduction peaks confirms the electroactive nature of the complexes. A relatively higher binding affinity was observed for the interaction of SS-DNA with complexes 2–6 compared to L1and L2. The findings of the DNA interaction study indicate an intercalative mode of interaction. The maximum inhibition against acetylcholinesterase enzyme was caused for complex 2 (IC50 = 2 µg/mL) compared to the standard drug Glutamine (IC50 = 2.10 µg/mL) while the maximum inhibition was found for butyrylcholinesterase enzyme by complex 4 (IC50 = 3 µg/mL) compared to the standard drug Glutamine (IC50 = 3.40 µg/mL). The findings of the enzymatic activity suggest that the under study compounds have potential for curing of Alzheimer’s disease. Similarly, complexes 2 and 4 possess the maximum inhibition as revealed from the free radical scavenging activity performed against DPPH and H2O2.

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Section: Resultsmentioning

confidence: 99%