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  Interaction of the adhesive protein Mefp-1 and fibrinogen with methyl and oligo (ethylene glycol)-terminated self-assembled monolayers

Harder, P., Grunze, M., & Waite, J. (2000). Interaction of the adhesive protein Mefp-1 and fibrinogen with methyl and oligo (ethylene glycol)-terminated self-assembled monolayers. Journal of Adhesion, 73(2-3), 161-177. doi:10.1080/00218460008029304.

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Harder, P., Author
Grunze, M.1, Author           
Waite, J.H., Author
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1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              

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Free keywords: Adhesion of proteins on alkanethiol self assembled monolayers (SAM), Oligo (ethylene oxide) terminated SAMs, Fibrinogen, FT-IRRS, Adhesive protein Mefp-1, Protein resistant surfaces
 Abstract: The interaction of fibrinogen and Mefp-1, the adhesive protein of the common blue mussel Mytilus edulis, with methyl- and oligo(ethylene oxide) (OEG)-terminated self-assembled monolayers (SAMs) has been investigated by Fourier Transform Infrared Reflection (FT-IRAS) analysis. The measurements on the hydrophobic surfaces show that the underlying SAM is structurally undisturbed when the proteins adhere. Mefp-1 is used as an attachment factor (Cell-TakTM) in cell cultures and in biomedical applications, and it is of interest to determine if OEG-terminated surfaces are inert towards Cell-Tak-mediated cell adhesion. We find that, when Langmuir transfer of a protein film at the liquid/air interface is avoided, the moderately hydrophilic hydroxyhexa (ethylene oxide) and methoxytri(ethylene oxide) undecanethiolate SAMs prepared on Au substrates are protein resistant. The inertness of the OEG-terminated surfaces does not depend on any specific protein present in solution, but rather appears to be a general phenomenon that is independent of the specific structure or chemistry of the macromolecule.

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Language(s): eng - English
 Dates: 2000-03-091999-11-202000-03-092006-09-232000
 Publication Status: Issued
 Pages: 17
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1080/00218460008029304
 Degree: -

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Title: Journal of Adhesion
Source Genre: Journal
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Publ. Info: London : Gordon and Breach
Pages: - Volume / Issue: 73 (2-3) Sequence Number: - Start / End Page: 161 - 177 Identifier: ISSN: 0021-8464
CoNE: https://pure.mpg.de/cone/journals/resource/954925409798