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Title: Characterisation of the protein corona using tunable resistive pulse sensing: determining the change and distribution of a particle’s surface charge
Authors: Blundell, Emma L.C.J.
Healey, Matthew J.
Holton, Elizabeth
Sivakumaran, Muttuswamy
Mastana, Sarabjit S.
Platt, Mark
Keywords: Biosensor
Zeta potential
Protein corona
Tunable pores
Issue Date: 2016
Publisher: Springer Verlag / © The Authors
Citation: BLUNDELL, E. ... et al, 2016. Characterisation of the protein corona using tunable resistive pulse sensing: determining the change and distribution of a particle’s surface charge. Analytical and Bioanalytical Chemistry, 408 (21), pp. 5757-5768.
Abstract: The zeta potential of the protein corona around carboxyl particles has been measured using tunable resistive pulse sensing (TRPS). A simple and rapid assay for characterising zeta potentials within buffer, serum and plasma is presented monitoring the change, magnitude and distribution of proteins on the particle surface. First, we measure the change in zeta potential of carboxyl-functionalised nanoparticles in solutions that contain biologically relevant concentrations of individual proteins, typically constituted in plasma and serum, and observe a significant difference in distributions and zeta values between room temperature and 37 °C assays. The effect is protein dependent, and the largest difference between the two temperatures is recorded for the γ-globulin protein where the mean zeta potential changes from −16.7 to −9.0 mV for 25 and 37 °C, respectively. This method is further applied to monitor particles placed into serum and/or plasma. A temperature-dependent change is again observed with serum showing a 4.9 mV difference in zeta potential between samples incubated at 25 and 37 °C; this shift was larger than that observed for samples in plasma (0.4 mV). Finally, we monitor the kinetics of the corona reorientation for particles initially placed into serum and then adding 5 % (V/V) plasma. The technology presented offers an interesting insight into protein corona structure and kinetics of formation measured in biologically relevant solutions, i.e. high protein, high salt levels, and its particle-by-particle analysis gives a measure of the distribution of particle zeta potential that may offer a better understanding of the behaviour of nanoparticles in solution.
Description: This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http:/ / creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
Sponsor: The work was supported by the European Commission for Research (PCIG11-GA-2012-321836 Nano4Bio) and the Peterborough City Hospital Haematology Research Fund. E.L.C.J.B. is supported by Izon Science Ltd and Loughborough University. EH was funded by the Analytical Science Trust fund for a summer studentship.
Version: Published
DOI: 10.1007/s00216-016-9678-6
URI: https://dspace.lboro.ac.uk/2134/21690
Publisher Link: http://dx.doi.org/10.1007/s00216-016-9678-6
ISSN: 1618-2650
Appears in Collections:Published Articles (Chemistry)

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