Protein adsorption onto polyester surfaces: is there a need for surface activation?
Surface hydrolysis of polyester scaffolds is a convenient technique suggested to promote protein adsorption for improving cell attachment. We have, therefore, investigated the effect of hydrolysis of polyester surfaces for protein adsorption to clarify the conditions needed. Three polyesters, poly(ethylene terephthalate) (PET), poly(lactic acid) (PLA), and poly(glycolic acid) (PGA), were selected. Adsorption was investigated by X-ray photoelectron spectroscopy (XPS), scanning electron microscopy (SEM), and quartz crystal microbalance (QCM). Hydrolyzed PET adsorbed significantly more proteins than nonhydrolyzed. Degradable polymers adsorbed at higher rates when the polymers were hydrolyzed prior to adsorption, but the same amount as nonhydrolyzed, suggesting spontaneous hydrolysis during the adsorption. XPS shows that hydrolysis prior to absorption for PET results in a surface nitrogen composition of approximately 14%, similar to pure protein (16%). Nonhydrolyzed PET surfaces showed only approximately 7% nitrogen, indicating protein layers thinner than approximately 10 nm. Adsorption to PLA and PGA shows nitrogen contents of 14-15% in both cases. SEM revealed striking differences in morphology of the protein coating. Hydrolyzed or spontaneously hydrolyzable surfaces display a pronounced fibrous structure while nonhydrolyzed surfaces give smooth structures. In combination, the results show that surface hydrolysis increase adsorption rate, but not the amount of proteins on polyesters that degrades in vivo. Surface treatment of nondegradable polyester increases the total amount of proteins and induces the formation of fibrous protein structures. Post hydrolysis treatment by acetic acid, replacing the counter-ion to a proton, further enhances protein attachment. Finally, cell attachment experiments verifies that protein adsorption increase the cell attachment to polyester surfaces.
Atthoff
Björn
B
Polymer Chemistry, Department of Materials Chemistry, Uppsala University, Box 538, 75121 Uppsala, Sweden.
Hilborn
Jöns
J