scholarly journals Multistable interaction between a spherical Brownian particle and an air–water interface

Soft Matter ◽  
2020 ◽  
Vol 16 (4) ◽  
pp. 960-969
Author(s):  
Stefano Villa ◽  
Antonio Stocco ◽  
Christophe Blanc ◽  
Maurizio Nobili
Keyword(s):  
Brownian Particle ◽  
Fluid Interfaces ◽  
Water Interface ◽  
Air Water Interface

A novel multi-stable interaction between microparticles and fluid interfaces is measured pointing out the still unaccounted role of surface heterogeneities.

Critical role of nanocomposites at air–water interface: From aqueous foams to foam-based lightweight functional materials

2021 ◽  
Vol 416 ◽  
pp. 129121
Author(s):  
Kai Yu ◽  
Bin Li ◽  
Huagui Zhang ◽  
Zhentao Wang ◽  
Wei Zhang ◽  
...  
Keyword(s):  
Critical Role ◽  
Functional Materials ◽  
Water Interface ◽  
Aqueous Foams ◽  
Air Water Interface

Specific ion adsorption at the air/water interface: The role of hydrophobic solvation

2009 ◽  
Vol 479 (4-6) ◽  
pp. 173-183 ◽  
Author(s):  
Dominik Horinek ◽  
Alexander Herz ◽  
Lubos Vrbka ◽  
Felix Sedlmeier ◽  
Shavkat I. Mamatkulov ◽  
...  
Keyword(s):  
Ion Adsorption ◽  
Water Interface ◽  
Air Water Interface ◽  
Specific Ion Adsorption ◽  
Hydrophobic Solvation

scholarly journals Cholesterol provides nonsacrificial protection of membrane lipids from chemical damage at air–water interface

2018 ◽  
Vol 115 (13) ◽  
pp. 3255-3260 ◽  
Author(s):  
Xinxing Zhang ◽  
Kevin M. Barraza ◽  
J. L. Beauchamp
Keyword(s):  
Lipid Membranes ◽  
Membrane Lipids ◽  
Oh Radicals ◽  
Significant Finding ◽  
Water Interface ◽  
Unsaturated Lipids ◽  
Air Water Interface ◽  
Liquid Ordered ◽  
Ester Linkage

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.

Organization of Microgels at the Air–Water Interface under Compression: Role of Electrostatics and Cross-Linking Density

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

Role of Tail−Tail Interactions versus Head-Group−Subphase Interactions in Pressure−Area Isotherms of Fatty Amines at the Air−Water Interface. 2. Time Dependence

Langmuir ◽  
1997 ◽  
Vol 13 (20) ◽  
pp. 5440-5446 ◽  
Author(s):  
P. Ganguly ◽  
D. V. Paranjape ◽  
K. R. Patil ◽  
Murali Sastry ◽  
F. Rondelez
Keyword(s):  
Time Dependence ◽  
Head Group ◽  
Water Interface ◽  
Fatty Amines ◽  
Air Water Interface ◽  
Pressure Area

scholarly journals Effect of the Air-Water Interface on the Conformation of Amyloid Beta

2020 ◽  
Author(s):  
Suman Samantray ◽  
David Cheung
Keyword(s):  
Conformational Change ◽  
Amyloid Beta ◽  
Md Simulation ◽  
Experimental Studies ◽  
Water Interface ◽  
Air Water Interface ◽  
Protein Conformational Change ◽  
Protein Fibrillation ◽  
Insight Into

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.

scholarly journals Effect of the Air-Water Interface on the Conformation of Amyloid Beta

2020 ◽  
Author(s):  
Suman Samantray ◽  
David Cheung
Keyword(s):  
Conformational Change ◽  
Amyloid Beta ◽  
Md Simulation ◽  
Experimental Studies ◽  
Water Interface ◽  
Air Water Interface ◽  
Protein Conformational Change ◽  
Protein Fibrillation ◽  
Insight Into

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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