Interactions of cephalexin with bovine serum albumin: displacement reaction and molecular docking

Abstract

Introduction: The drug-plasma protein interaction is a fundamental issue in guessing and checking the serious drug side effects related with other drugs. The purpose of this research was to study the interaction of cephalexin with bovine serum albumin (BSA) and displacement reaction using site probes. Methods: The interaction mechanism concerning cephalexin (CPL) with BSA was investigated using various spectroscopic methods and molecular modeling method. The binding sites number, n, apparent binding constant, K, and thermodynamic parameters, ΔG0, ΔH0, and ΔS0 were considered at different temperatures. To evaluate the experimental results, molecular docking modeling was calculated. Results: The distance, r=1.156 nm between BSA and CPL were found in accordance with the Forster theory of non-radiation energy transfer (FRET) indicating energy transfer occurs between BSA and CPL. According to the binding parameters and ΔG0= negative values and ΔS0= 28.275 j mol-1K-1, a static quenching process is effective in the CPL-BSA interaction spontaneously. ΔG0 for the CPL-BSA complex obtained from the docking simulation is -28.99 kj mol-1, which is close to experimental ΔG of binding, -21.349 kj mol-1 that indicates a good agreement between the results of docking methods and experimental data. Conclusion: The outcomes of spectroscopic methods revealed that the conformation of BSA changed during drug-BSA interaction. The results of FRET propose that CPL quenches the fluorescence of BSA by static quenching and FRET. The displacement study showed that phenylbutazon and ketoprofen displaced CPL, indicating that its binding site on albumin is site I and Gentamicin cannot be displaced from the binding site of CPL. All results of molecular docking method agreed with the results of experimental data.

Probing the interactions of novel europium coordination complexes with serum albumin

“…The intrinsic fluorescence of BSA was largely attributed to two tryptophan residues – Trp134 and Trp213. [ 17,18 ] Multiple tyrosines and phenylalanines have been shown to make a minor contribution to the overall spectrum, depending on the wavelength selected for excitation. The results of the quenching studies (Figure 4) were quantitatively analyzed within the framework of the Stern–Volmer model (Equation 2).…”

Comprehensive Assessment of Biomolecular Interactions of Morpholine‐Based Mixed Ligand Cu(II) and Zn(II) Complexes of 2,2′‐Bipyridine as Potential Anticancer and SARS‐CoV‐2 Agents: A Synergistic Experimental and Structure‐Based Virtual Screening

“…When increasing the sample concentrations, the BSA intensity diminishes dramatically owing to static quenching in the ground state. It is noted that the fuorophores of BSA are not clearly exposed to a shift in polarity [74][75][76]. Te fuorescence spectra of bovine serum albumin with a variety of concentrations of all samples were estimated, and they are displayed in Figure S26.…”

Exploring The Interactions of a Natural Gamma-Oryzanol with Human Serum Albumin: Surface Plasmon Resonance, Fluorescence, and Molecular Modeling Studies

“…To study the structural changes of HSA in the presence of ORY and BSA-ORY complex formation, UV-Vis absorption measurements were performed [18,19]. UV absorption spectra of HSA in the absence and presence of ORY are shown in ▶ Fig.…”