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

Chowdhury, Megha Sen; Gümüş, Selçuk; Dasgupta, Sanchari; Majumder, Ishani; Bhattacharya, Amartya Kumar; Das, Debasis; Mukhopadhyay, Jayanta; Bose, Debosreeta; Dasgupta, Saumya; Akınay, Yüksel; Mukhopadhyay, Jayanta

doi:10.1002/open.202200033

Cited by 6 publications

(2 citation statements)

References 24 publications

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“…Arg144 in cleft of domains IB, IIIA, and IIIB in BSA . Leu189A has a hydrophobic side chain, while Arg144A has a positively charged group, but both these amino acid residues are observed to form hydrophobic interaction with ANSA.…”

Section: Resultsmentioning

confidence: 97%

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Analytical Aspects of ANSA–BSA Association: A Thermodynamic and Conformational Approach

Jain,

Judy,

Kishore

2024

J. Phys. Chem. B

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Many studies have demonstrated the manner in which ANS interacts with bovine serum albumin (BSA), although they are limited by the extremely low solubility of dye. The present study demonstrates the binding of ANSA dye with BSA, and since this dye can easily replace ANS, it not only simplifies research but also improves sensor accuracy for serum albumin. A combination of calorimetry and spectroscopy has been employed to establish the thermodynamic signatures associated with the interaction of ANSA with the protein and the consequent conformational changes in the latter. The results of differential scanning calorimetry reveal that when the concentration of ANSA in solution is increased, the thermal stability of the protein increases substantially. The fluorescence data demonstrated a decrease in the binding affinity of ANSA with the protein when pH increased but was unable to identify a change in the mode of interaction of the ligand. ITC has demonstrated that the mode of interaction between ANSA and the protein varies from a single set of binding sites at pH 5 and 7.4 to a sequential binding site at pH 10, emphasizing the potential relevance of protein conformational changes. TCSPC experiments suggested a dynamic type in the presence of ANSA. Molecular docking studies suggest that ANSA molecules are able to find ionic centers in the hydrophobic pockets of BSA. The findings further imply that given its ease of use in experiments, ANSA may be a useful probe for tracking the presence of serum albumin and partially folded protein states.

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Section: Resultsmentioning

confidence: 97%

“…75 Arg144 in cleft of domains IB, IIIA, and IIIB in BSA. 76 Leu189A has a hydrophobic side chain, while Arg144A has a positively charged group, 77 but both these amino acid residues are observed to form hydrophobic interaction with ANSA. The arginine molecule cluster in aqueous solution exhibits a hydrophobic surface by aligning its three methylene groups.…”

mentioning

confidence: 99%

Analytical Aspects of ANSA–BSA Association: A Thermodynamic and Conformational Approach

Jain,

Judy,

Kishore

2024

J. Phys. Chem. B

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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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DFT Analyses of arsylsemicarbazone group as functional compound for application as excellent fluorescent probes and medicament: study on virtual screening through molecular docking

Bose,

Sil,

Chakraborty

et al. 2024

Chem. Pap.

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The present invention reports two novel functional compounds, 2-hydroxy-3-naphthaldehyde thiosemicarbazone (2H3NTS) and 2-hydroxy-3-naphthaldehyde semi carbazone (2H3NS) as an excellent uorescent probe which possess anticancer features and are not yet synthesized by any research group.The DFT study reveals signi cantly higher stokes shift (315 nm) for 2H3NS indicating swift relaxation from initial to the emissive state and reduces self-quenching from self-molecular absorption which favours its practical application. Consequently, successive in-vitro activity of 2H3NTS and /2H3NS is studied using molecular docking towards the inhibition capacity of target kinase protein like CDK, primarily responsible for cell growth. As expected, 2H3NS is capable of binding both competitive ATP binding SITE I and non-competitive SITE II which lies below the T-loop, thereby inhibiting the cell growth and differentiation. However, 2H3NTS with polarizable sulphur is incapable of binding at SITE I with selective inhibition posing the ATP site to be well conserved.

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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

Cited by 6 publications

References 24 publications

Analytical Aspects of ANSA–BSA Association: A Thermodynamic and Conformational Approach

Analytical Aspects of ANSA–BSA Association: A Thermodynamic and Conformational Approach

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

DFT Analyses of arsylsemicarbazone group as functional compound for application as excellent fluorescent probes and medicament: study on virtual screening through molecular docking

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