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Binding interaction study on human serum albumin with bactericidal gold nanoparticles synthesized from a leaf extract of Musa balbisiana : a multispectroscopic approach
Author(s) -
Maji Anukul,
Beg Maidul,
Das Somnath,
Sahoo Nandan Kumar,
Jha Pradeep K.,
Islam Md. Maidul,
Hossain Maidul
Publication year - 2019
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.3639
Subject(s) - dynamic light scattering , fourier transform infrared spectroscopy , circular dichroism , nanoparticle , human serum albumin , chemistry , spectroscopy , zeta potential , binding constant , nuclear chemistry , quenching (fluorescence) , transmission electron microscopy , analytical chemistry (journal) , fluorescence spectroscopy , ultraviolet visible spectroscopy , fluorescence , colloidal gold , materials science , chromatography , crystallography , nanotechnology , chemical engineering , biochemistry , organic chemistry , binding site , physics , quantum mechanics , engineering
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.