Penetration of Insoluble Lipid Monolayers at the Air−Water Interface by Water-Soluble Block Copolymers and Homopolymers

Langmuir ◽  
1997 ◽  
Vol 13 (21) ◽  
pp. 5524-5527 ◽  
Author(s):  
James R. Charron ◽  
Robert D. Tilton
1998 ◽  
Vol 31 (22) ◽  
pp. 7877-7885 ◽  
Author(s):  
S. W. An ◽  
R. K. Thomas ◽  
F. L. Baines ◽  
N. C. Billingham ◽  
S. P. Armes ◽  
...  

2009 ◽  
Vol 7 (suppl_1) ◽  
Author(s):  
Rakesh Kumar Harishchandra ◽  
Mohammed Saleem ◽  
Hans-Joachim Galla

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.


2014 ◽  
Vol 550 ◽  
pp. 621-629 ◽  
Author(s):  
Rute I.S. Romão ◽  
José M.G. Martinho ◽  
Amélia M.P.S. Gonçalves da Silva

Langmuir ◽  
2018 ◽  
Vol 34 (21) ◽  
pp. 6095-6108 ◽  
Author(s):  
Katharina Widder ◽  
Jennica Träger ◽  
Andreas Kerth ◽  
George Harauz ◽  
Dariush Hinderberger

1995 ◽  
Vol 269 (4) ◽  
pp. L492-L497 ◽  
Author(s):  
T. M. McEachren ◽  
K. M. Keough

The influence of the acute inflammatory phase protein human C-reactive protein (CRP) on the adsorption of porcine pulmonary surfactant from a subphase into an air-water interface has been investigated. CRP was shown to detract from the ability of surfactant to rapidly adsorb to the air-water interface at a molar ratio of 0.03:1 (protein:phospholipid) (weight ratio, 0.5:1). On a weight basis, CRP was found to be more effective than fibrinogen at reducing the adsorption rate of surfactant. The effect of CRP required the presence of calcium and was reversed by the addition of phosphocholine in a concentration-dependent manner. The inhibition of surfactant adsorption by CRP was effectively eliminated by the addition of phosphocholine at a molar ratio of 300:1 (phosphocholine:CRP), but it was not diminished by the addition of identical molar ratios of o-phosphoethanolamine or DL-alpha-glycerophosphate at the same molar ratios. These data suggest that the potent inhibition of surfactant adsorption by CRP is primarily a result of a specific interaction between CRP and the phosphocholine headgroup of surfactant lipids in the subphase and that it can be reversed by the water-soluble CRP ligand, phosphocholine.


2002 ◽  
Vol 4 (11) ◽  
pp. 2329-2336 ◽  
Author(s):  
José M. Pedrosa ◽  
Marta Pérez ◽  
Inmaculada Prieto ◽  
María Teresa Martín-Romero ◽  
Dietmar Möbius ◽  
...  

2001 ◽  
Vol 388 (1-2) ◽  
pp. 5-8 ◽  
Author(s):  
Yasushi Umemura ◽  
Akihiko Yamagishi ◽  
Robert Schoonheydt ◽  
André Persoons ◽  
Frans De Schryver

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