In-situ studies of protein-resistant self-assembling monolayers

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Oligo(ethylene glycol) (OEG) SAMs are important tools in medical applications to hinder the irreversible adsorption of proteins on surfaces. They can be used to structure cells on surfaces or in combination with specific headgroups as sensor elements. The aim of this work was the in-situ characterization of hexa(ethylene glycol) self-assembling monolayers (SAMs), their structural changes at elevated temperatures and their longtime stability. The focus was on the interaction of the thiol molecules with the surrounding water molecules and the conformational and structural consequences. A key to the understanding of the mechanism of protein resistance is the ability of OEG-SAMs to bind water molecules at their surface and in their interior. Infrared spectroscopy is a well suited technique for the identification of molecules and their structural changes due to the interaction with their environment. The surface sensitive polarization modulation infrared reflection absorption spectroscopy (PMIRRAS) technique enables in combination with a thin liquid layer cell measurements under aqueous conditions (in-situ) with a very high signal-to-noise ratio.

Autorentext

09 / 2000 - 05 / 2006 Diploma in Physics, Friedrich Schiller University Jena, Center for molecular biomedicine 08 / 2006 - 10 / 2010 Ph.D studies at the Eberhard Karls University of Tu bingen, Institute of applied physics Since 01 / 2011 Postdoctoral researcher at the University of Wisconsin-Madison, Wisconsin Institute for Medical Research

Weitere Informationen

  • Allgemeine Informationen
    • GTIN 09783838122687
    • Sprache Englisch
    • Größe H220mm x B150mm x T10mm
    • Jahr 2010
    • EAN 9783838122687
    • Format Kartonierter Einband (Kt)
    • ISBN 978-3-8381-2268-7
    • Titel In-situ studies of protein-resistant self-assembling monolayers
    • Autor Stefan Zorn
    • Untertitel Polarisation Modulation Infrared Spectroscopy measurements under aqueous conditions
    • Gewicht 255g
    • Herausgeber Südwestdeutscher Verlag
    • Anzahl Seiten 160
    • Genre Biologie

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