X-ray and neutron reflectivity studies of a protein monolayer adsorbed to a functionalized aqueous surface

Vaknin, David; Kjaer, K.; Ringsdorf, Helmut; Blankenburg, R.; Piepenstock, M.; Diederich, Anke; Lösche, Mathias

doi:10.1021/la00029a003

Cited by 44 publications

(27 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Clearly, increasing biotin density induces protein adsorption to rise although the thickness of the protein layer remains fixed at $4 nm, consistent with the size of SA. 20,25,26,31,42,43 At the highest biotin densities, the electron density of this layer is found to saturate at <r>/r buffer ¼ 1.18 AE 0.02, in agreement with the previously obtained values for the 2D crystals of lipid-supported SA. 43 The excess density <r>/r buffer -1 > 0 for the protein layer provides a direct measure of the amount of proteins adsorbed.…”

Section: Resultssupporting

confidence: 90%

Effects of surface ligand density on lipid-monolayer-mediated 2D assembly of proteins

et al. 2010

View full text Add to dashboard Cite

Section: Resultssupporting

confidence: 90%

Effects of surface ligand density on lipid-monolayer-mediated 2D assembly of proteins

et al. 2010

View full text Add to dashboard Cite

“…The low fitted Hamaker constant was attributed to the small area of molecular contact between the Fab' and opposed bilayer surface due to the low Fab' surface coverage and to the protein's intrinsic roughness. With a Fab'-streptavidin stoichiometry of 1:1 Ebato et al, 1994), and a streptavidin surface coverage of 45.0 ± 0.5 nm2/streptavidin (Vaknin et al, 1993;, the calculated Fab' charge based on these measurements was 0.2 unit charge/Fab'. Despite the overall negative Fab' charge, the negative fluorescein membrane electrostatic potential ensured that the measured electrostatic surface potential of the Fab' monolayer was unambiguously positive (Leckband et al, 1994).…”

Section: Resultsmentioning

confidence: 99%

4-4-20 Anti-Fluorescyl IgG Fab' Recognition of Membrane Bound Hapten: Direct Evidence for the Role of Protein and Interfacial Structure

Kuhl

et al. 1995

Biochemistry

View full text Add to dashboard Cite

The surface forces apparatus was used to identify the molecular forces that control the interactions of monoclonal 4-4-20 antifluorescyl IgG Fab' fragments with fluorescein-presenting supported planar bilayers. At long range, the electrostatic force between oriented Fab' and fluorescein monolayers was controlled by the composition of the protein exterior surrounding the antigen-combining site rather than by the overall protein charge. The measured positive electrostatic potential of the Fab' monolayer at pH > pI(Fab') was consistent with the structure of the exposed Fab' surface in which a ring of positive charge at the mouth of the antigen-combining site dominates the local electrostatic surface properties. Substantial differences in the electrostatic forces measured with denatured Fab' further demonstrated that the measured electrostatic surface properties and the consequent long-range interaction forces are controlled by the protein surface composition. At short range, the strength of the Fab'-mediated adhesion was modulated not only by the length of the fluorescein tether but also by membrane hydration. Steric hydration barriers at the membrane surface reduced the adhesion strength in proportion to their range of influence. These results provide direct evidence that long-range protein interactions with immobilized ligands are controlled by both the protein and the membrane surface compositions, while short-range, specific binding is modulated by both the protein structure and the membrane interfacial properties.

show abstract

“…XR and NR techniques are recently being applied to the liquid systems. However, most of them use a strong X-ray source from synchrotron radiation (SR) − and neutrons, ,, which are very limited in use for experimentalists in related fields. Some investigators have developed the XR apparatus for the study of a monolayer on a water surface with a rotating anode X-ray generator. − In 1996, Yamaoka et al succeeded in constructing a specially designed XR apparatus for the study of a monolayer on a water surface for laboratory use. − This apparatus has a Langmuir−Blodgett (LB) trough at the sample position; hence, the structure of the monolayer on a water surface can be studied as a function of the surface pressure, directly.…”

Section: Introductionmentioning

confidence: 99%

Direct in Situ Observation of a Lipid Monolayer−DNA Complex at the Air−Water Interface by X-ray Reflectometry

et al. 1999

View full text Add to dashboard Cite

Direct in situ observation of the fine structure of the cationic lipid monolayer−DNA complex on a water surface has been carried out by using an air−water interface X-ray reflectivity (XR) instrument. Interestingly, the thickness of the DNA layer was markedly thinner than the geometry of the cylindrical DNA molecule when the complex was deposited on the solid substrates; the thickness was determined to be 11 Å by XR measurement in a dried state, while the diameter of the DNA molecule is about 24 Å. However, the thickness in the complex on a water surface was estimated by in situ XR measurement to be about 25−28 Å, which is comparable to the geometry of the DNA molecule. Thus, the anomalously thin thickness was due to some experimental treatments, such as deposition on a solid substrate and/or drying. The structure of the monolayer and monolayer−polymer complex on the solid substrates in a dried state is not the same as that on a water surface. The possibility of some dynamic fluctuation of its structure was also suggested. These results strongly indicate the importance of a direct in situ study such as by the XR technique for the structural study of the monolayer and monolayer complex on a water surface.

show abstract

X-ray and neutron reflectivity studies of a protein monolayer adsorbed to a functionalized aqueous surface

Cited by 44 publications

References 0 publications

Effects of surface ligand density on lipid-monolayer-mediated 2D assembly of proteins

Effects of surface ligand density on lipid-monolayer-mediated 2D assembly of proteins

4-4-20 Anti-Fluorescyl IgG Fab' Recognition of Membrane Bound Hapten: Direct Evidence for the Role of Protein and Interfacial Structure

Direct in Situ Observation of a Lipid Monolayer−DNA Complex at the Air−Water Interface by X-ray Reflectometry

Contact Info

Product

Resources

About