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Protein & Peptide Letters

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ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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Research Article

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

Author(s): Anchal Sharma and Kalyan Sundar Ghosh*

Volume 27, Issue 8, 2020

Page: [793 - 800] Pages: 8

DOI: 10.2174/0929866527666200129123018

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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 106 -1010 M-1 and the quenching constant was determined as ~107 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 nanoparticles with BLG, which also causes structural perturbations of the protein.

Keywords: Bovine β-lactoglobulin, silver nanoparticles, fluorescence quenching, 3D-fluorescence, circular dichroism, synchronous fluorescence.

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