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Issue 7, 2018
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The interaction of silver nanoparticles with papain and bromelain

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Abstract

Proteins cover the surface of nanoparticles (NPs), forming what is known as a “protein corona”, which largely determines the reactivity and functionality of NPs. In the study, a comprehensive investigation was performed for clarifying the binding mechanism, adsorption isotherms and kinetic behaviors of silver nanoparticles (AgNPs) with two model cysteine-proteases, papain and bromelain. The experimental results indicate that the binding of papain/bromelain to AgNPs seems to be a static quenching mechanism. Thermodynamic analysis reveals that the binding of papain/bromelain to AgNPs is synergistically driven by enthalpy and entropy, and the major driving forces are hydrophobic and electrostatic interactions. The equilibrium adsorption isotherm and kinetics of papain/bromelain on AgNPs were also studied. The adsorption equilibrium isotherms both fit well to the Freundlich model and the kinetics of adsorption both fit best to pseudo-second-order.

Graphical abstract: The interaction of silver nanoparticles with papain and bromelain

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Publication details

The article was received on 08 Dec 2017, accepted on 12 Feb 2018 and first published on 12 Feb 2018


Article type: Paper
DOI: 10.1039/C7NJ04847E
Citation: New J. Chem., 2018,42, 4940-4950
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    The interaction of silver nanoparticles with papain and bromelain

    X. Li, Z. Yang and Y. Peng, New J. Chem., 2018, 42, 4940
    DOI: 10.1039/C7NJ04847E

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