Binding interaction study on human serum albumin with bactericidal gold nanoparticles synthesized from a leaf extract of Musa balbisiana: a multispectroscopic approach

Abstract

This study describes the eco-friendly, low-cost and room-temperature synthesis of gold nanoparticles from Musa balbisiana leaf extract, which acts as both reducing and stabilizing agent, and characterized by ultraviolet−visible (UV-vis) light spectroscopy, fourier transform infrared (FTIR) spectroscopy, field emission scanning electron microscopy (FE-SEM), analytical transmission electron microscopy (TEM), energy-dispersive X-ray spectroscopy (EDAX) and dynamic light scattering (DLS) instruments. These nanoparticles showed an average diameter of 33.83 ± 3.39 nm, which was confirmed from the size distribution histogram. The bactericidal activity of these nanoparticles was confirmed using bacteria Escherichia coli and Staphylococcus aureus at 1 and 2 nM minimum inhibitory concentrations, respectively. The interaction between nanoparticles and human serum albumin (HSA) was investigated, as this plays significant roles in biological systems. The nature of interaction, binding parameters and structural variation of HSA in the presence of these nanoparticles have been evaluated using several useful spectroscopic approaches such as UV-vis, FTIR, time-resolved and steady-state fluorescence, and circular dichroism in addition to the measurement of zeta potential.This interaction study revealed that static quenching occurs in this process with minimal alteration in the secondary structure, but the native structure of HSA remained unaltered. The binding constant and thermodynamic parameters of this interaction process were also evaluated.

Localized Surface Plasmon Resonance as a Tool to Study Protein Corona Formation on Nanoparticles

“…For example, it was employed to study the PC formation of human serum albumin on eco-friendly AuNPs synthesized using aqueous leaf extracts from therapeutic plant Nymphaea nouchali or Musa balbisiana. 99,100 In a different work, the deposition of BSA on Au NPs was followed. 101 The analysis of Stern−Volmer plots for the interaction of glycosylated human transferrin and nonglycosylated recombinant human transferrin with Au NPs also confirmed that these proteins form stable complexes with NPs and the fluorescence is quenched following the static mechanism.…”

Brief Research on the Biophysical Study and Anticancer Behavior of Pt(II) Complexes: Their DNA/BSA Binding, Molecular Docking, and Cytotoxic Property

“…54 Again "peak-2" at λ excitation = 230 and λ emission = 341 indicates the polypeptide backbone structures of BSA. 53 Both "peak-1" and "peak-2" of BSA decrease with one time addition of 10 μM complexes (Pt-1−Pt-4). The decrease of intensity indicates the conformational changes of the polypeptide backbone structure of BSA, which is due to a change in the microenvironment at the vicinity of either or both tryptophan and tyrosine residues.…”

Multi‐spectroscopic, thermodynamic and molecular docking studies to investigate the interaction of eplerenone with human serum albumin

“…[ 36 ] Several investigations on the interaction of small molecules and drugs to HSA have been recently published. [ 37–42 ] To the best of our knowledge, no previous research has been published on the intermolecular binding interactions of EPL with serum albumin using several spectroscopic and molecular docking approaches.…”

“…[36] Several investigations on the interaction of small molecules and drugs to HSA have been recently published. [37][38][39][40][41][42] To the best of our Standard stock solution of HSA (2.0 μM) was freshly prepared and obtained by weighing 0.0133 g of HSA and then dissolving in distilled water in a volumetric flask (100 ml). The 20.0 mM Trishydrochloric acid (HCl) buffer (pH 7.4) was obtained by weighing 0.24 g of Tris and dissolving it in distilled water in a volumetric flask (100 mL).…”