Probing resistance to protein adsorption of oligo(ethylene glycol)- terminated self-assembled monolayers by scanning force microscopy

K. Feldman, G. Hähner*, N. D. Spencer, P. Harder, M. Grunze

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

244 Citations (Scopus)

Abstract

Functionalized scanning force microscope (SFM) probes were used to investigate and to mimic the interaction between fibrinogen and self- assembled monolayers (SAMs) of methoxytri(ethylene glycol) undecanethiolates -S(CH2)11(OCH2CH2)3OCH3 (EG3-OMe) on gold and silver surfaces. The SAMs on gold are resistant to protein adsorption, whereas the films on silver adsorb variable amounts of fibrinogen. Experiments were performed with both charged and hydrophobic tips as models for local protein structures to determine the influence of these parameters on the interaction with the SAMs. A striking difference between the two monolayers was established when the forces were measured in an aqueous environment with hydrophobic probes. While a long-range attractive hydrophobic interaction was observed for the EG3-OMe on silver, a repulsive force was measured for EG3- OMe on gold. The strong dependence of the repulsive force for the EG3-OMe- gold system upon the solution ionic strength suggests that this interaction has a significant electrostatic contribution. The observed differences are attributed to the distinct molecular conformations of the oligo(ethylene glycol) tails on the gold-supported (helical) and silver-supported ('all- trans') monolayers. A comparison of the force/distance curves for the EG3-OMe SAMs with those measured under identical conditions on end-grafted poly(ethylene glycol) (PEG 2000) on gold further emphasizes that the nature of the repulsive forces originating from the short-chain oligomers is unique and not related to a 'steric repulsion' effect.

Original languageEnglish
Pages (from-to)10134-10141
Number of pages8
JournalJournal of the American Chemical Society
Volume121
Issue number43
DOIs
Publication statusPublished - 3 Nov 1999

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