Interactions between Protein Coated Particles and Polymer Surfaces Studied with the Rotating Particles Probe

• Published in: Langmuir Vol. 28; no. 21; pp. 8149 - 8155
• Main Authors: Kemper, M, Spridon, D, van IJzendoorn, L. J, Prins, M. W. J
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 29-05-2012
• Subjects: Chemistry; Coated Materials, Biocompatible - chemistry; Exact sciences and technology; General and physical chemistry; Magnetite Nanoparticles - chemistry; Myoglobin - chemistry; Particle Size; Polystyrenes - chemistry; Surface Properties; Shape; Model study; Polymer; Protein; Energy; Ionic strength; Biosensor; Distribution; Coated particle; pH; Styrene polymer; Models; Oxidation; Magnetic field; Interaction parameter
• ISSN: 0743-7463; 1520-5827
• DOI: 10.1021/la300630n

Nonspecific interactions between proteins and polymer surfaces have to be minimized in order to control the performance of biosensors based on immunoassays with particle labels. In this paper we investigate these nonspecific interactions by analyzing the response of protein coated magnetic particles to a rotating magnetic field while the particles are in nanometer vicinity to a polymer surface. We use the fraction of nonrotating (bound) particles as a probe for the interaction between the particles and the surface. As a model system, we study the interaction of myoglobin coated particles with oxidized polystyrene surfaces. We measure the interaction as a function of the ionic strength of the solution, varying the oxidation time of the polystyrene and the pH of the solution. To describe the data we propose a model in which particles bind to the polymer by crossing an energy barrier. The height of this barrier depends on the ionic strength of the solution and two interaction parameters. The fraction of nonrotating particles as a function of ionic strength shows a characteristic shape that can be explained with a normal distribution of energy barrier heights. This method to determine interaction parameters paves the way for further studies to quantify the roles of protein coated particles and polymers in their mutual nonspecific interactions in different matrixes.