Unveiling the interaction, cytotoxicity and antibacterial potential of pyridine derivatives: an experimental and theoretical approach with bovine serum albumin.

Autor: Das R; School of Biotechnology, Gangadhar Meher University, Sambalpur, Odisha, 768001, India., Mohanty P; Department of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur, Odisha, 768018, India., Dash PP; Department of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur, Odisha, 768018, India., Mishra S; Department of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur, Odisha, 768018, India., Bishoyi AK; Department of Clinical Hematology, Institute of Medical Sciences and SUM Hospital, Siksha 'O' Anusandhan Deemed University, Bhubaneswar, Odisha, 751003, India., Mishra L; Department of Life Science, National Institute of Technology, Rourkela, 769008, India., Prusty L; Department of Chemistry, National Institute of Technology, Rourkela, 769008, India., Behera DP; Department of Chemistry, National Institute of Technology, Rourkela, 769008, India., Dubey D; Medical Research Laboratory, Institute of Medical Sciences and SUM Hospital, Siksha 'O' Anusandhan Deemed University, Bhubaneswar, Odisha, 751003, India., Mishra M; Department of Life Science, National Institute of Technology, Rourkela, 769008, India., Sahoo H; Department of Chemistry, National Institute of Technology, Rourkela, 769008, India., Khan MS; Department of Biochemistry, College of Science, King Saud University, Riyadh, 11451, Saudi Arabia., Sethi SK; School of Biotechnology, Gangadhar Meher University, Sambalpur, Odisha, 768001, India. sksethi2k@gmail.com., Jali BR; Department of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur, Odisha, 768018, India. bigyan.Jali7@gmail.com.
Jazyk: angličtina
Zdroj: Naunyn-Schmiedeberg's archives of pharmacology [Naunyn Schmiedebergs Arch Pharmacol] 2024 Nov 01. Date of Electronic Publication: 2024 Nov 01.
DOI: 10.1007/s00210-024-03541-6
Abstrakt: 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.
(© 2024. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.)
Databáze: MEDLINE
Externí odkaz: