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The interaction of silver nanoparticles with papain and bromelain


Proteins cover the surface of nanoparticles (NPs), forming what is known as “protein corona”, largely determine 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 papain/bromelain binds 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.

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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, Accepted Manuscript
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    The interaction of silver nanoparticles with papain and bromelain

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

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