Protein adsorption to poly(ethylene oxide) surfaces
Article first published online: 13 SEP 2004
Copyright © 1991 John Wiley & Sons, Inc.
Journal of Biomedical Materials Research
Volume 25, Issue 12, pages 1547–1562, December 1991
How to Cite
Gombotz, W. R., Guanghui, W., Horbett, T. A. and Hoffman, A. S. (1991), Protein adsorption to poly(ethylene oxide) surfaces. J. Biomed. Mater. Res., 25: 1547–1562. doi: 10.1002/jbm.820251211
- Issue published online: 13 SEP 2004
- Article first published online: 13 SEP 2004
- Manuscript Accepted: 12 JUN 1991
- Manuscript Received: 23 MAY 1990
Surfaces containing poly(ethylene oxide) (PEO) are interesting biomaterials because they exhibit low degrees of protein adsorption and cell adhesion. In this study different molecular weight PEO molecules were covalently attached to poly(ethylene terephthalate) (PET) films using cyanuric chloride chemistry. Prior to the PEO immobilization, amino groups were introduced onto the PET films by exposing them to an allylamine plasma glow discharge. The amino groups on the PET film were next activated with cyanuric chloride and then reacted with bis- amino PEO. The samples were characterized by scanning electron microscopy, water contact angle measurements, gravimetric analysis, and electron spectroscopy for chemical analysis (ESCA). The adsorption of 125I-labeled baboon fibrinogen and bovine serum albumin was studied from buffer solutions. Gravimetric analysis indicated that the films grafted with the low-molecularweight PEO contained many more PEO molecules than the surfaces grafted with higher-molecular-weight PEO. The highmolecular-weight PEO surfaces, however, exhibited greater wettability (lower water contact angles) and less protein adsorption than the low-molecular-weight PEO surfaces. Adsorption of albumin and fibrinogen to the PEO surfaces decreased with increasing PEO molecular weight up to 3500. A further increase in molecular weight resulted in only slight decreases in protein adsorption. Protein adsorption studies as a function of buffer ionic strength suggest that there may be an ionic interaction between the protein and the allylamine surface. The trends in protein adsorption together with the water contact angle results and the gravimetric analysis suggest that a kind of “cooperative” water structuring around the larger PEO molecules may create an “excluded volume” of the hydrated polymer coils. This may be an important factor contributing to the observed low protein adsorption behavior.