Surface charge effects in protein adsorption on nanodiamonds

Aramesh, M; Shimoni, O; Ostrikov, K; Prawer, S; Cervenka, J

Surface charge effects in protein adsorption on nanodiamonds

Aramesh, M Shimoni, O

Ostrikov, K Prawer, S Cervenka, J

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Publication Type:: Journal Article
Citation:: Nanoscale, 2015, 7 (13), pp. 5726 - 5736
Issue Date:: 2015-04-07

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Field	Value	Language
dc.contributor.author	Aramesh, M	en_US
dc.contributor.author	Shimoni, O https://orcid.org/0000-0001-8822-1024	en_US
dc.contributor.author	Ostrikov, K	en_US
dc.contributor.author	Prawer, S	en_US
dc.contributor.author	Cervenka, J	en_US
dc.date.issued	2015-04-07	en_US
dc.identifier.citation	Nanoscale, 2015, 7 (13), pp. 5726 - 5736	en_US
dc.identifier.issn	2040-3364	en_US
dc.identifier.uri	http://hdl.handle.net/10453/35342
dc.description.abstract	© The Royal Society of Chemistry. Understanding the interaction of proteins with charged diamond nanoparticles is of fundamental importance for diverse biomedical applications. Here we present a thorough study of protein binding, adsorption kinetics and structure on strongly positively (hydrogen-terminated) and negatively (oxygen-terminated) charged nanodiamond particles using a quartz crystal microbalance by dissipation and infrared spectroscopy. By using two model proteins (bovine serum albumin and lysozyme) of different properties (charge, molecular weight and rigidity), the main driving mechanism responsible for the protein binding to the charged nanoparticles was identified. Electrostatic interactions were found to dominate the protein adsorption dynamics, attachment and conformation. We developed a simple electrostatic model that can qualitatively explain the observed adsorption behaviour based on charge-induced pH modifications near the charged nanoparticle surfaces. Under neutral conditions, the local pH around the positively and negatively charged nanodiamonds becomes very high (11-12) and low (1-3) respectively, which has a profound impact on the protein charge, hydration and affinity to the nanodiamonds. Small proteins (lysozyme) were found to form multilayers with significant conformational changes to screen the surface charge, while larger proteins (albumin) formed monolayers with minor conformational changes. The findings of this study provide a step forward toward understanding and eventually predicting nanoparticle interactions with biofluids. This journal is	en_US
dc.relation.ispartof	Nanoscale	en_US
dc.relation.isbasedon	10.1039/c5nr00250h	en_US
dc.subject.classification	Nanoscience & Nanotechnology	en_US
dc.subject.mesh	Proteins	en_US
dc.subject.mesh	Materials Testing	en_US
dc.subject.mesh	Binding Sites	en_US
dc.subject.mesh	Protein Binding	en_US
dc.subject.mesh	Adsorption	en_US
dc.subject.mesh	Surface Properties	en_US
dc.subject.mesh	Models, Chemical	en_US
dc.subject.mesh	Models, Molecular	en_US
dc.subject.mesh	Computer Simulation	en_US
dc.subject.mesh	Nanodiamonds	en_US
dc.title	Surface charge effects in protein adsorption on nanodiamonds	en_US
dc.type	Journal Article
utslib.citation.volume	13	en_US
utslib.citation.volume	7	en_US
utslib.for	0912 Materials Engineering	en_US
utslib.for	0306 Physical Chemistry (incl. Structural)	en_US
utslib.for	02 Physical Sciences	en_US
utslib.for	03 Chemical Sciences	en_US
utslib.for	10 Technology	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Mathematical and Physical Sciences
pubs.organisational-group	/University of Technology Sydney/Strength - IBMD - Initiative for Biomedical Devices
utslib.copyright.status	closed_access
pubs.issue	13	en_US
pubs.publication-status	Published	en_US
pubs.volume	7	en_US

Abstract:

© The Royal Society of Chemistry. Understanding the interaction of proteins with charged diamond nanoparticles is of fundamental importance for diverse biomedical applications. Here we present a thorough study of protein binding, adsorption kinetics and structure on strongly positively (hydrogen-terminated) and negatively (oxygen-terminated) charged nanodiamond particles using a quartz crystal microbalance by dissipation and infrared spectroscopy. By using two model proteins (bovine serum albumin and lysozyme) of different properties (charge, molecular weight and rigidity), the main driving mechanism responsible for the protein binding to the charged nanoparticles was identified. Electrostatic interactions were found to dominate the protein adsorption dynamics, attachment and conformation. We developed a simple electrostatic model that can qualitatively explain the observed adsorption behaviour based on charge-induced pH modifications near the charged nanoparticle surfaces. Under neutral conditions, the local pH around the positively and negatively charged nanodiamonds becomes very high (11-12) and low (1-3) respectively, which has a profound impact on the protein charge, hydration and affinity to the nanodiamonds. Small proteins (lysozyme) were found to form multilayers with significant conformational changes to screen the surface charge, while larger proteins (albumin) formed monolayers with minor conformational changes. The findings of this study provide a step forward toward understanding and eventually predicting nanoparticle interactions with biofluids. This journal is

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http://hdl.handle.net/10453/35342