Dewetting of adsorbed protein on polystyrene and graphite surfaces during drying

Philip J. Lowe; Andrew Badley; David C. Cullen

doi:10.1117/12.350620

17 June 1999 Dewetting of adsorbed protein on polystyrene and graphite surfaces during drying

Philip J. Lowe, Andrew Badley, David C. Cullen

Proceedings Volume 3607, Scanning and Force Microscopies for Biomedical Applications; (1999) https://doi.org/10.1117/12.350620
Event: BiOS '99 International Biomedical Optics Symposium, 1999, San Jose, CA, United States

Abstract

The physical adsorption and subsequent drying of biomolecules on surfaces is a common manufacturing step throughout the bio-diagnostics industry. To address the lack of knowledge concerning the molecular details of such commercially important processes, we have studied the effect of drying on absorbed layers of protein using the AFM. AFM images of adsorbed layers of monoclonal antibody on polystyrene microtitre plates after drying exhibited non- homogeneous distributions of protein reminiscent of the de- wetted structures often seen with polymer thin-films. Variation of the drying rate resulted in notably different protein distributions at micrometer and sub-micrometer scales. No obvious effect on the polystyrene microtitre plate nano-topography on the de-wetted distributions of antibody was apparent. To further explore the possible effects of nano-topography on the de-wetted distributions of antibodies and other proteins during drying, highly oriented pyrolytic graphite, with a surface topography consisting of hydrophobic basal plane areas disrupted by edge plane defects, has been studied. For this surface, de-wetting during drying of adsorbed antibody and bovine serum albumin layers appears to be significantly influenced by the edge plane defects including specific parameters such as the edge plane defect density.

Citation Download Citation

Philip J. Lowe, Andrew Badley, and David C. Cullen "Dewetting of adsorbed protein on polystyrene and graphite surfaces during drying", Proc. SPIE 3607, Scanning and Force Microscopies for Biomedical Applications, (17 June 1999); https://doi.org/10.1117/12.350620

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