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Nanoparticle–protein interactions: Water is the key

Published online by Cambridge University Press:  12 December 2014

Daniel F. Moyano ,
Moumita Ray  and
Vincent M. Rotello
Daniel F. Moyano
Affiliation:
Department of Chemistry, University of Massachusetts Amherst, USA; dmoyano@chem.umass.edu
Moumita Ray
Affiliation:
Department of Chemistry, University of Massachusetts Amherst, USA; moumita@chem.umass.edu
Vincent M. Rotello
Affiliation:
Department of Chemistry, University of Massachusetts Amherst, USA; rotello@chem.umass.edu
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Abstract

Nanoparticle (NP) surface properties define how engineered nanomaterials interact with proteins. In aqueous systems, these interactions are driven by the binding of water to NPs and proteins. Understanding the true nature of this NP–water interface and its involvement in the properties of nanomaterials is a fundamental challenge in nanotechnology. Here, we review recent studies on the involvement of water molecules in the interaction of NPs with proteins. We first address the thermodynamic aspects of the NP–protein interaction and the means by which solvation shells can alter the nature of this phenomenon. We then discuss how the chemical nature of the NP surface affects the adsorption of water molecules and how this adsorption can either favor or inhibit protein–NP interactions.

Keywords

nanoscalesurface chemistrywaterbiologicaladsorption
Type
Research Article
Information
MRS Bulletin , Volume 39 , Issue 12: Water at Functional Interfaces , December 2014 , pp. 1069 - 1073
Copyright
Copyright © Materials Research Society 2014 

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