Protein Interactions with Bottle-Brush Polymer Layers: Effect of Side Chain and Charge Density Ratio Probed by QCM-D and AFM
2010 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 349, no 1, 265-274 p.Article in journal (Refereed) Published
Silica surfaces were coated with a range of cationic bottle-brush polymers with 45 units long poly(ethylene oxide) side chains, and their efficiency in reducing protein adsorption was probed by QCM-D, reflectometry and AFM. Preadsorbed layers formed by bottle-brush polymers with different side chain to charge ratio was exposed to two proteins with different net charge, lysozyme and BSA. The reduction in protein adsorption was found to depend on both the type of protein and on the nature of the polyelectrolyte layer. The most pronounced reduction in protein adsorption was achieved when the fraction of charged backbone segments was in the range 0.25-0.5 equivalent to a fraction of poly(ethylene oxide) side chains of 0.75-0.5. It was concluded that these polymers have enough electrostatic attachment points to ensure a strong binding to the surface, and at the same time a sufficient amount of poly(ethylene oxide) side chains to counteract protein adsorption. In contrast, a layer formed by a highly charged polyelectrolyte without side chains was unable to resists protein adsorption. On such a layer the adsorption of negatively charged BSA was strongly enhanced, and positively charged lysozyme adsorbed to a similar extent as to bare silica. AFM colloidal probe force measurement between silica surfaces with preadsorbed layers of bottle-brush polymers were conducted before and after exposure to BSA and lysozyme to gain insight into how proteins were incorporated in the bottle-brush polymer layers.
Place, publisher, year, edition, pages
2010. Vol. 349, no 1, 265-274 p.
Protein repellency, Protein adsorption, Surface forces, AFM, QCM-D, Reflectometry, BSA, Lysozyme, Bottle-brush polymer
IdentifiersURN: urn:nbn:se:kth:diva-14003DOI: 10.1016/j.jcis.2010.05.061ISI: 000279966700036ScopusID: 2-s2.0-77954175021OAI: oai:DiVA.org:kth-14003DiVA: diva2:329004
FunderSwedish Research Council
QC 20100707 Uppdaterad från submitted till published (20110204).2010-07-072010-07-072011-02-04Bibliographically approved