Unprecedented biological evaluation of Zn(II) complexes supported by “Self-adjustable” acyclic diiminodipyrromethane Schiff’s bases: DFT, molecular docking; biological activity studies

Loke, Shiva Krishna; Pagadala, Eswar; Srinivasadesikan, Venkatesan; Thanapaul, Rex Jeya Rajkumar Samdavid; Pooventhiran, T.; Thomas, Renjith; Naganjaneyulu, G.; Kottalanka, Ravi K.

doi:10.1016/j.inoche.2021.108936

Cited by 8 publications

(2 citation statements)

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“…[6][7][8] Shiva Krishnaloke et al synthesized Zn diiminodipyrromethane Schiff bases complexes for in vitro cytotoxicity and antibacterial activities using cancer cells. [9] Ajmeera Ramesh et al has reported biological activity of Schiff bases of 4aminoantipyrine with copper(II), zinc(II), nickel(II), and cobalt(II) metals. The obtained results showed that Schiff bases of 4aminoantipyrine with Zn metals displayed the best antimicrobial activity compared with other metal complexes ligands.…”

Section: Introductionmentioning

confidence: 99%

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Supramolecular Arrangement and DFT analysis of Zinc(II) Schiff Bases: An Insight towards the Influence of Compartmental Ligands on Binding Interaction with Protein

et al. 2022

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We report, for the first time, a detailed crystallographic study of the supramolecular arrangement for a set of zinc(II) Schiff base complexes containing the ligand 2,6-bis((E)-((2-(dimethylamino)ethyl)imino)methyl)-4-R-phenol], where R = methyl/tertbutyl/chloro. The supramolecular study acts as a pre-screening tool for selecting the compartmental ligand R of the Schiff base for effective binding with a targeted protein, bovine serum albumin (BSA). The most stable hexagonal arrangement of the complex [ZnÀ Me] (R = Me) stabilises the ligand with the highest FMO energy gap (ΔE = 4.22 eV) and lowest number of conformations during binding with BSA. In contrast, formation of unstable 3D columnar vertebra for [ZnÀ Cl] (R = Cl) tend to activate the system with lowest FMO gap (3.75 eV) with highest spontaneity factor in molecular docking. Molecular docking analyses reported in terms of 2D LigPlot + identified site A, a cleft of domains IB, IIIA and IIIB, as the most probable protein binding site of BSA. Arg144, Glu424, Ser428, Ile455 and Lys114 form the most probable interactions irrespective of the type of compartmental ligands R of the Schiff base whereas Arg185, Glu519, His145, Ile522 act as the differentiating residues with ΔG = À 7.3 kcal mol À 1 .

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Section: Introductionmentioning

confidence: 99%

“…Shiva Krishnaloke et al. synthesized Zn diiminodipyrromethane Schiff bases complexes for in vitro cytotoxicity and antibacterial activities using cancer cells [9] . Ajmeera Ramesh et al.…”

Section: Introductionmentioning

confidence: 99%