NDLI: Characterisation of the protein corona using tunable resistive pulse sensing: determining the change and distribution of a particle’s surface charge

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Characterisation of the protein corona using tunable resistive pulse sensing: determining the change and distribution of a particle’s surface charge

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Characterisation of the protein corona using tunable resistive pulse sensing: determining the change and distribution of a particle’s surface charge

Content Provider	Springer Nature Link
Author	Blundell, Emma L. C. J. Healey, Matthew J. Holton, Elizabeth Sivakumaran, Muttuswamy Manstana, Sarabjit Platt, Mark
Copyright Year	2016
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. Graphical Abstract The relative velocity of a nanoparticle as it traverses a nanopore can be used to determine its zeta potential. Monitoring the changes in translocation speeds can therefore be used to follow changes to the surface chemistry/composition of 210 nm particles that were placed into protein rich solutions, serum and plasma. The particle-by-particle measurements allow the zeta potential and distribution of the particles to be characterised, illustrating the effects of protein concentration and temperature on the protein corona. When placed into a solution containing a mixture of proteins, the affinity of the protein to the particle’s surface determines the corona structure, and is not dependent on the protein concentration
Starting Page	5757
Ending Page	5768
Page Count	12
File Format	PDF
ISSN	16182642
Journal	Analytical and Bioanalytical Chemistry
Volume Number	408
Issue Number	21
e-ISSN	16182650
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2016-06-10
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biosensor TRPS Zeta potential Protein corona Tunable pores Analytical Chemistry Biochemistry Laboratory Medicine Characterization and Evaluation of Materials Food Science Monitoring/Environmental Analysis
Content Type	Text
Resource Type	Article
Subject	Analytical Chemistry Biochemistry

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Characterisation of the protein corona using tunable resistive pulse sensing: determining the change and distribution of a particle’s surface charge

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Characterisation of the protein corona using tunable resistive pulse sensing: determining the change and distribution of a particle’s surface charge

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Characterisation of the protein corona using tunable resistive pulse sensing: determining the change and distribution of a particle’s surface charge

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Characterisation of the protein corona using tunable resistive pulse sensing: determining the change and distribution of a particle’s surface charge