Dilational rheology of an air–water interface functionalized by biomolecules: the role of surface diffusion

2006 ◽  
Vol 45 (4) ◽  
pp. 497-504 ◽  
Author(s):  
Cyril Picard ◽  
Laurent Davoust
2021 ◽  
Vol 416 ◽  
pp. 129121
Author(s):  
Kai Yu ◽  
Bin Li ◽  
Huagui Zhang ◽  
Zhentao Wang ◽  
Wei Zhang ◽  
...  

2009 ◽  
Vol 479 (4-6) ◽  
pp. 173-183 ◽  
Author(s):  
Dominik Horinek ◽  
Alexander Herz ◽  
Lubos Vrbka ◽  
Felix Sedlmeier ◽  
Shavkat I. Mamatkulov ◽  
...  

2018 ◽  
Vol 115 (13) ◽  
pp. 3255-3260 ◽  
Author(s):  
Xinxing Zhang ◽  
Kevin M. Barraza ◽  
J. L. Beauchamp

The role of cholesterol in bilayer and monolayer lipid membranes has been of great interest. On the biophysical front, cholesterol significantly increases the order of the lipid packing, lowers the membrane permeability, and maintains membrane fluidity by forming liquid-ordered–phase lipid rafts. However, direct observation of any influence on membrane chemistry related to these cholesterol-induced physical properties has been absent. Here we report that the addition of 30 mol % cholesterol to 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) or 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (POPG) monolayers at the air–water interface greatly reduces the oxidation and ester linkage cleavage chemistries initiated by potent chemicals such as OH radicals and HCl vapor, respectively. These results shed light on the indispensable chemoprotective function of cholesterol in lipid membranes. Another significant finding is that OH oxidation of unsaturated lipids generates Criegee intermediate, which is an important radical involved in many atmospheric processes.


2016 ◽  
Vol 294 (10) ◽  
pp. 1577-1584 ◽  
Author(s):  
Houjian Gong ◽  
Long Xu ◽  
Teng Zhu ◽  
Guiying Xu ◽  
Xiaofeng Shi ◽  
...  

Langmuir ◽  
2017 ◽  
Vol 33 (32) ◽  
pp. 7968-7981 ◽  
Author(s):  
Christine Picard ◽  
Patrick Garrigue ◽  
Marie-Charlotte Tatry ◽  
Véronique Lapeyre ◽  
Serge Ravaine ◽  
...  

2005 ◽  
Vol 109 (27) ◽  
pp. 13327-13331 ◽  
Author(s):  
R. Miller ◽  
M. E. Leser ◽  
M. Michel ◽  
V. B. Fainerman

Langmuir ◽  
1997 ◽  
Vol 13 (20) ◽  
pp. 5440-5446 ◽  
Author(s):  
P. Ganguly ◽  
D. V. Paranjape ◽  
K. R. Patil ◽  
Murali Sastry ◽  
F. Rondelez

2020 ◽  
Author(s):  
Suman Samantray ◽  
David Cheung

Using MD simulation the conformation of the fibril forming protein amyloid beta at the air-water interface. It is found that adsorption at the air-water interface induces the formation of aggregation prone alpha-helical conformations, consistent with experimental studies of amyloid beta. Adsorption on the air-water interface also reduces the number of distinct conformations that the protein exhibits. This provides insight into the role of protein conformational change into the enhancement of protein fibrillation at interfaces.


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