Deutsch
 
Benutzerhandbuch Datenschutzhinweis Impressum Kontakt
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

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

MPG-Autoren
/persons/resource/persons211638

Grunze,  M.
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

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.


Zitierlink: http://hdl.handle.net/21.11116/0000-0001-BAB7-F
Zusammenfassung
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.