Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/14106

TitleProtein adsorption to oligo (Ethylene Glycol) self assembled monolayers with amide linkage experiments with fibrinogen, heparinised plasma and serum
Author(s)Benesch, Johan
Svedhem, S.
Svensson, S. C.
Valiokas, R.
Liedberg, B.
Tengvall, P.
KeywordsSelf-assembled monolayers
Oligo(ethylene glycol)
Protein adsorption
Fibrinogen
Heparinized plasma
Serum
Complement
Issue date2001
JournalJournal of Biomaterials Science. Polymer Edition
Abstract(s)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 brinogen, serum, and plasma were studied by ellipsometry on a series of well-de ned 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 D 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 brinogen adsorbing from a single protein solution, but larger amounts of proteins from serum and plasma. The adsorption of brinogen and blood plasma decreased with an increasing number of EG repeats and was temperature-dependent. Signi cantly less serum adsorbed to methoxy tri(EG) than to hexa(EG) and more proteins remained on the latter surface after incubation in a sodiumdodecyl 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 surfacemediated complement activationwas observed. The present study points to the importance of a careful choice of the proteinmodel system before general statements regardingthe protein repellantproperties of potential surfaces can be made.
TypeArticle
URIhttp://hdl.handle.net/1822/14106
ISSN0920-5063
Peer-Reviewedyes
AccessOpen access
Appears in Collections:3B’s - Artigos em revistas/Papers in scientific journals

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