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Studies on Molecular Interactions between Bovine Β-Lactoglobulin and Silver Nanoparticles

Author(s):

Anchal Sharma and Kalyan Sundar Ghosh*   Pages 1 - 8 ( 8 )

Abstract:


Background: Silver nanoparticles (AgNPs) were found to modulate the fibrillation of bovine β-lactoglobulin (BLG).

Objective: To gain an insight regarding the mechanism of BLG aggregation modulation by AgNPs at molecular level, studies on the interactions between BLG and AgNPs were carried out.

Methods: Protein-ligand interactions were studied based on Trp fluorescence quenching (at four different temperatures), synchronous and three-dimensional fluorescence and circular dichroism spectroscopy (far-UV and near-UV).

Results: Protein-nanoparticles association constant was in the range of 10 6 -10 10 M -1 and the quenching constant was determined as ~10 7 M-1. Ground state complexation between the protein and nanoparticles was predicted. Change in polarity surrounding the Trp residue was not detected by synchronous and three-dimensional fluorescence spectroscopy. AgNPs caused a global change in the secondary and tertiary structure of the protein as revealed from far-UV and near-UV CD spectroscopy. Enthalpy driven complexation between the protein and nanoparticles indicates the involvement of hydrogen bonding and/or van der Waals interactions.

Conclusion: Modulation of BLG aggregation by AgNPs is due to strong binding of the nanopartilces with BLG, which also causes structural perturbations of the protein.

Keywords:

Bovine β-lactoglobulin, Silver nanoparticles, Fluorescence quenching, 3D-fluorescence, Circular dichroism, Synchronous fluorescence

Affiliation:

Department of Chemistry, National Institute of Technology Hamirpur, Himachal Pradesh 177005, Department of Chemistry, National Institute of Technology Hamirpur, Himachal Pradesh 177005



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