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Protein adsorption onto polyester surfaces: Is there a need for surface activation?
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Materials Chemistry, Polymer Chemistry.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Materials Chemistry, Polymer Chemistry.
2007 (English)In: Journal of Biomedical Materials Research - Part B Applied Biomaterials, ISSN 1552-4973, Vol. 80, no 1, 121-130 p.Article in journal (Refereed) Published
Abstract [en]

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 noehydrolyzed, suggesting spontaneous hydrolysis during the adsorption. XPS shows that hydrolysis prior to absorption for PET results in a surface nitrogen composition of ∼14%, similar to pure protein (16%). Nonhydrolyzed PET surfaces showed only ∼7% nitrogen, indicating protein layers thinner than ∼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.

Place, publisher, year, edition, pages
2007. Vol. 80, no 1, 121-130 p.
Keyword [en]
Poly(ethylene terephtalate), Poly(glycolic acid), Poly(lactic acid), Protein adsorption, Surface modification, Surface treatment
National Category
Chemical Sciences
URN: urn:nbn:se:uu:diva-94592DOI: 10.1002/jbm.b.30576ISI: 000243018200015PubMedID: 16680692OAI: oai:DiVA.org:uu-94592DiVA: diva2:168488
Available from: 2006-05-17 Created: 2006-05-17 Last updated: 2011-02-22Bibliographically approved
In thesis
1. Tailoring of Biomaterials using Ionic Interactions: Synthesis, Characterization and Application
Open this publication in new window or tab >>Tailoring of Biomaterials using Ionic Interactions: Synthesis, Characterization and Application
2006 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The interactions between polymers and components of biological systems are an important area of interest within the fields of tissue engineering, polymer chemistry, medicine and biomaterials. In order to create such a biomimetic material, it must show the inherent ability to reproduce or elicit a biological function. How do we design synthetic materials in order to direct their interactions with biological systems?

This thesis contributes to this research with aspects of how polymers interact with biological materials with the help of ionic interactions. Polyesters, biodegradable or not, may after a hydrolytic cleavage interact ionically with protonated amines by the liberated carboxylate functions. Amines are found in proteins and this fact will help us to anchor proteins to polyester surfaces. Another type of interaction is to culture cells in polymeric materials, i.e. scaffolds. We have been working on compliant substrates, knitted structures, to allow cell culture in three dimensions. A problem that arises here is how to get a high cell seeding efficiency? By working on the interactions between polymers, proteins and finally cells, it is possible to create a polarized protein membrane that allows for very efficient cell seeding, and subsequent three dimensional cell cultures. Finally a synthetic route to taylor interaction was developed. Here a group of polymers known as ionomers were synthesized. In our case ionic end groups have been placed onto biodegradable polycarbonates, we have created amphiphilic telechelic ionomers. Functionalization, anionic or cationic, changes the properties of the material in many ways due to aggregation and surface enrichment of ionic groups. It is possible to add functional groups for a variety of different interactions, for example introducing ionic groups that interact and bind to the complementary charge of proteins or on the other hand one can chose groups to prevent protein interactions, like the phosphorylcholine zwitterionomers. Such interactions can be utilized to modulate the release of proteins from these materials when used in protein delivery applications. The swelling properties, Tg, degradation rate and mechanical properties are among other things that will easily be altered with the choice of functional groups or backbone polymer.

Place, publisher, year, edition, pages
Uppsala: Acta Universitatis Upsaliensis, 2006. 92 p.
Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, ISSN 1651-6214 ; 193
Chemistry, biodegradable polymers, ionomer, water uptake, protein delivery, protein adsorption, protein membrane, cell seeding efficiency, amphiphillic, inner structure, polarized membrane, Kemi
urn:nbn:se:uu:diva-6924 (URN)91-554-6585-4 (ISBN)
Public defence
2006-06-07, Polhemsalen, Ångströmlaboratoriet, Regementsvägen 1, Uppsala, 10:00
Available from: 2006-05-17 Created: 2006-05-17 Last updated: 2013-09-26Bibliographically approved

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