Protein adsorption to oligo(ethylene glycol) self-assembled monolayers: Experiments with fibrinogen, heparinized plasma, and serum
2001 (English)In: Journal of Biomaterials Science. Polymer Edition, ISSN 0920-5063, Vol. 12, no 6, 581-597 p.Article in journal (Refereed) Published
Low protein adsorption is believed advantageous for blood-contacting materials and ethylene glycols (EG)-based polymeric compounds are often attached to surfaces for this purpose. In the present study, the adsorption of fibrinogen, serum, and plasma were studied by ellipsometry on a series of well-defined oligo(EG) terminated alkane-thiols self-assembled on gold. The layers were prepared with compounds of the general structure HS-(CH2)15-CONH-EGn, where n = 2, 4, and 6. Methoxy-terminated tri(EG) undecanethiol and hydroxyl-terminated hexadecanethiol self-assembled monolayers (SAMs) were used as references. The results clearly demonstrate that the adsorption depends on the experimental conditions with small amounts of fibrinogen adsorbing from a single protein solution, but larger amounts of proteins from serum and plasma. The adsorption of fibrinogen and blood plasma decreased with an increasing number of EG repeats and was temperature-dependent. Significantly less serum adsorbed to methoxy tri(EG) than to hexa(EG) and more proteins remained on the latter surface after incubation in a sodium dodecyl sulfate (SDS) solution, indicating a looser protein binding to the methoxy-terminated surface. All surfaces adsorbed complement factor 3(C3) from serum and plasma, although no surface-mediated complement activation was observed. The present study points to the importance of a careful choice of the protein model system before general statements regarding the protein repellant properties of potential surfaces can be made.
Place, publisher, year, edition, pages
2001. Vol. 12, no 6, 581-597 p.
Complement, Fibrinogen, Heparinized plasma, Oligo(ethylene glycol), Protein adsorption, Self-assembled monolayers, Serum
Engineering and Technology
IdentifiersURN: urn:nbn:se:liu:diva-47265DOI: 10.1163/156856201316883421OAI: oai:DiVA.org:liu-47265DiVA: diva2:268161