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Unveiling the interaction, cytotoxicity and antibacterial potential of pyridine derivatives: an experimental and theoretical approach with bovine serum albumin
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Unveiling the interaction, cytotoxicity and antibacterial potential of pyridine derivatives: an experimental and theoretical approach with bovine serum albumin
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Journal Article
Unveiling the interaction, cytotoxicity and antibacterial potential of pyridine derivatives: an experimental and theoretical approach with bovine serum albumin
2025
Overview
The binding interactions between bovine serum albumin (BSA) and three pyridine derivatives, i.e., 2-(5-bromopyridin-3-yl) acetic acid (
L1
), 3-bromo-5-nitropyridine (
L2
) and 2-chloro-4-nitropyridine (
L3
), have been carried out using UV-Vis and fluorescence spectroscopic methods. Fluorescence intensity quenching is observed by adding
L2
and
L3
to the BSA solution. The quenched fluorescence emission is due to the static nature. An isothermal titration calorimetry (ITC) experiment shows the binding ability of
L1
with BSA. The binding constants are found to be 7.23 ± 0.32 × 10
5
M
−1
for
L1
. The thermodynamic parameters were calculated from ITC measurements (i.e., ∆H = −2.78 ± 0.08 kcal/mol, ∆G = −5.65 ± 0.25 kcal/mol, and -T∆S = −2.87 ± 0.11 kcal/mol), which indicated that the protein-ligand complex formation between
L1
and BSA is mainly due to the hydrogen bonds and van der Waals interactions. Cyclic voltammetry (CV) and structure activity and relationship (SAR) studies have been carried out to establish the relationship between ligands and proteins. Additionally, we conducted an antibacterial assay with gram-positive
Staphylococcus aureus
,
Enterococcus faecalis
, and negative bacterial strains
Acinetobacter baumannii
and
Escherichia coli
against
L1
,
L2
, and
L3
, aiming to address the challenges posed by the co-existence of multidrug-resistant bacteria. Finally, drosophila is used to test the cytotoxicity of ligands
L1
,
L2
, and
L3
’s in vitro.
Publisher
Springer Berlin Heidelberg,Springer Nature B.V
