Use of Total Reflection X-ray Fluorescence (TRXF) for the Quantification of DNA Binding to Lipid Monolayers at the Air−Water Interface

Langmuir ◽  
2010 ◽  
Vol 26 (18) ◽  
pp. 14766-14773 ◽  
Author(s):  
Vladimir L. Shapovalov ◽  
Matthias Dittrich ◽  
Oleg V. Konovalov ◽  
Gerald Brezesinski
Keyword(s):  
Dna Binding ◽  
Total Reflection ◽  
Lipid Monolayers ◽  
Water Interface ◽  
X Ray ◽  
Air Water Interface

scholarly journals Total Reflection X-Ray Fluorescence at the Air Water Interface using XeRay

2017 ◽  
Vol 112 (3) ◽  
pp. 175a
Author(s):  
Zhiliang Gong ◽  
Daniel Kerr ◽  
Hyeondo L. Hwang ◽  
J. Michael Henderson ◽  
Tiffany Suwatthee ◽  
...  
Keyword(s):  
Total Reflection ◽  
Water Interface ◽  
X Ray ◽  
Air Water Interface

An X-ray scattering study of lipid monolayers at the air-water interface and on solid supports

1988 ◽  
Vol 159 (1-2) ◽  
pp. 17-28 ◽  
Author(s):  
K. Kjaer ◽  
J. Als-Neilsen ◽  
C.A. Heln ◽  
P. Tippmann-Krayer ◽  
H. Möhwald
Keyword(s):  
Lipid Monolayers ◽  
Water Interface ◽  
Solid Supports ◽  
X Ray ◽  
X Ray Scattering ◽  
Air Water Interface ◽  
Scattering Study ◽  
Ray Scattering

X-ray Synchrotron Study of Packing and Protrusions of Polymer−Lipid Monolayers at the Air−Water Interface

1998 ◽  
Vol 120 (7) ◽  
pp. 1469-1473 ◽  
Author(s):  
J. Majewski ◽  
T. L. Kuhl ◽  
K. Kjaer ◽  
M. C. Gerstenberg ◽  
J. Als-Nielsen ◽  
...  
Keyword(s):  
Lipid Monolayers ◽  
Water Interface ◽  
X Ray ◽  
Air Water Interface

Zinc(II) Porphyrins at the Air−Water Interface As Studied by Polarized Total-Reflection X-ray Absorption Fine Structure

Langmuir ◽  
2006 ◽  
Vol 22 (1) ◽  
pp. 209-212 ◽  
Author(s):  
Hirohisa Nagatani ◽  
Hajime Tanida ◽  
Toru Ozeki ◽  
Iwao Watanabe
Keyword(s):  
Fine Structure ◽  
Total Reflection ◽  
Water Interface ◽  
X Ray ◽  
Absorption Fine ◽  
Air Water Interface ◽  
X Ray Absorption

X-ray Scattering Studies of Mixed Monolayers of Tetrakis(3,5-di-tert-butylphenyl)porphinatocopper(II) with Cadmium Arachidate at the Air/Water Interface

Langmuir ◽  
2000 ◽  
Vol 16 (17) ◽  
pp. 7051-7055 ◽  
Author(s):  
Jian Bang Peng ◽  
Gwen A. Lawrie ◽  
Geoffrey T. Barnes ◽  
Ian R. Gentle ◽  
Garry J. Foran ◽  
...  
Keyword(s):  
Water Interface ◽  
Mixed Monolayers ◽  
X Ray ◽  
X Ray Scattering ◽  
Air Water Interface ◽  
Ray Scattering

scholarly journals Nanoparticle interaction with model lung surfactant monolayers

2009 ◽  
Vol 7 (suppl_1) ◽  
Author(s):  
Rakesh Kumar Harishchandra ◽  
Mohammed Saleem ◽  
Hans-Joachim Galla
Keyword(s):  
Surface Properties ◽  
Self Assembly ◽  
Current Knowledge ◽  
Surface Film ◽  
Lung Surfactant ◽  
Hydrophobic Surface ◽  
Surface Pattern ◽  
Lipid Monolayers ◽  
Water Interface ◽  
Air Water Interface

One of the most important functions of the lung surfactant monolayer is to form the first line of defence against inhaled aerosols such as nanoparticles (NPs), which remains largely unexplored. We report here, for the first time, the interaction of polyorganosiloxane NPs (AmorSil20: 22 nm in diameter) with lipid monolayers characteristic of alveolar surfactant. To enable a better understanding, the current knowledge about an established model surface film that mimics the surface properties of the lung is reviewed and major results originating from our group are summarized. The pure lipid components dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylglycerol have been used to study the biophysical behaviour of their monolayer films spread at the air–water interface in the presence of NPs. Film balance measurements combined with video-enhanced fluorescence microscopy have been used to investigate the formation of domain structures and the changes in the surface pattern induced by NPs. We are able to show that NPs are incorporated into lipid monolayers with a clear preference for defect structures at the fluid–crystalline interface leading to a considerable monolayer expansion and fluidization. NPs remain at the air–water interface probably by coating themselves with lipids in a self-assembly process, thereby exhibiting hydrophobic surface properties. We also show that the domain structure in lipid layers containing surfactant protein C, which is potentially responsible for the proper functioning of surfactant material, is considerably affected by NPs.

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