Influence of surface chemistry on the structural organization of monomolecular protein layers adsorbed to functionalized aqueous interfaces

M. Lösche, M. Piepenstock, A. Diederich, T. Grunewald, K. Kjær, D. Vaknin

    Research output: Contribution to journalJournal articleResearch

    Abstract

    The molecular organization of streptavidin (SA) bound to aqueous surface monolayers of biotin-functionalized lipids and binary lipid mixtures has been investigated with neutron reflectivity and electron and fluorescence microscopy. The substitution of deuterons (2H) for protons (1H), both in subphase water molecules and in the alkyl chains of the lipid surface monolayer, was utilized to determine the interface structure on the molecular length scale. In all cases studied, the protein forms monomolecular layers underneath the interface with thickness values of apprx 40 ANG . A systematic dependence of the structural properties of such self-assembled SA monolayers on the surface chemistry was observed: the lateral protein density depends on the length of the spacer connecting the biotin moiety and its hydrophobic anchor. The hydration of the lipid head groups in the protein-bound state depends on the dipole moment density at the interface.
    Original languageEnglish
    JournalBiophysical Journal
    Volume65
    Issue number5
    Pages (from-to)2160-2177
    ISSN0006-3495
    Publication statusPublished - 1993

    Fingerprint Dive into the research topics of 'Influence of surface chemistry on the structural organization of monomolecular protein layers adsorbed to functionalized aqueous interfaces'. Together they form a unique fingerprint.

    Cite this