Journal article
Measurement of the Average Mass of Proteins Adsorbed to a Nanoparticle by Using a Suspended Microchannel Resonator
Journal of pharmaceutical sciences, Vol.104(2), pp.698-704
02/2015
DOI: 10.1002/jps.24206
PMID: 25318413
Abstract
We assessed the potential of a suspended microchannel resonator (SMR) to measure the adsorption of proteins to nanoparticles. Standard polystyrene beads suspended in buffer were weighed by a SMR system. Particle suspensions were mixed with solutions of bovine serum albumin (BSA) or monoclonal human antibody (IgG), incubated at room temperature for 3 h and weighed again with SMR. The difference in buoyant mass of the bare and protein-coated polystyrene beads was calculated into real mass of adsorbed proteins. The average surface area occupied per protein molecule was calculated, assuming a monolayer of adsorbed protein. In parallel, dynamic light scattering (DLS), nanoparticle tracking analysis (NTA), and zeta potential measurements were performed. SMR revealed a statistically significant increase in the mass of beads because of adsorption of proteins (for BSA and IgG), whereas DLS and NTA did not show a difference between the size of bare and protein-coated beads. The change in the zeta potential of the beads was also measurable. The surface area occupied per protein molecule was in line with their known size. Presented results show that SMR can be used to measure the mass of adsorbed protein to nanoparticles with a high precision in the presence of free protein. (c) 2014 Wiley Periodicals, Inc. and the American Pharmacists Association J Pharm Sci 104:698-704, 2015
Details
- Title: Subtitle
- Measurement of the Average Mass of Proteins Adsorbed to a Nanoparticle by Using a Suspended Microchannel Resonator
- Creators
- M. Reza Nejadnik - Leiden UniversityWim Jiskoot - Leiden University
- Resource Type
- Journal article
- Publication Details
- Journal of pharmaceutical sciences, Vol.104(2), pp.698-704
- DOI
- 10.1002/jps.24206
- PMID
- 25318413
- NLM abbreviation
- J Pharm Sci
- ISSN
- 0022-3549
- eISSN
- 1520-6017
- Publisher
- Wiley
- Number of pages
- 7
- Grant note
- 115363 / European Union; European Commission
- Language
- English
- Date published
- 02/2015
- Academic Unit
- Roy J. Carver Department of Biomedical Engineering; Pharmaceutical Sciences and Experimental Therapeutics
- Record Identifier
- 9984420943602771
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