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

• Published in: Luminescence (Chichester, England) England), 2019-09, Vol.34 (6), p.563-575
• Main Authors: Maji, Anukul, Beg, Maidul, Das, Somnath, Sahoo, Nandan Kumar, Jha, Pradeep K., Islam, Md. Maidul, Hossain, Maidul
• Format: Article
• Language: English
• Subjects: Albumin; Albumins; Analytical methods; Anti-Bacterial Agents - chemical synthesis; Anti-Bacterial Agents - chemistry; Anti-Bacterial Agents - pharmacology; Bacteria; Bactericidal activity; bactericidal property; Binding; Circular Dichroism; Dichroism; E coli; Electron microscopy; Emission analysis; Energy transmission; Escherichia coli - drug effects; Field emission microscopy; Field emission spectroscopy; Fluorescence; fluorescence studies; Fourier transforms; Gold; Gold - chemistry; Gold - pharmacology; Histograms; Human serum albumin; Humans; Infrared analysis; Infrared spectroscopy; Instruments; Interaction parameters; Leaves; Light scattering; Mathematical analysis; Metal Nanoparticles - chemistry; MGNs synthesis; MGNs–HSA conjugate; Microscopy; Musa - chemistry; Musa balbisiana; Nanoparticles; Parameters; Particle Size; Photon correlation spectroscopy; Plant extracts; Plant Extracts - chemistry; Plant Leaves - chemistry; Process parameters; Protein Binding; Protein structure; Scanning electron microscopy; Secondary structure; Serum; Serum albumin; Serum Albumin, Human - chemistry; Size distribution; Spectrophotometry, Ultraviolet; Spectroscopy; Spectroscopy, Fourier Transform Infrared; Spectrum analysis; Stabilizers (agents); Stabilizing; Staphylococcus aureus - drug effects; Transmission electron microscopy; Ultraviolet radiation; Zeta potential
• ISSN: 1522-7235; 1522-7243
• DOI: 10.1002/bio.3639

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.