scholarly journals E-Cadherin Tethered to Micropatterned Supported Lipid Bilayers as a Model for Cell Adhesion

Langmuir ◽  
2005 ◽  
Vol 21 (25) ◽  
pp. 11963-11968 ◽  
Author(s):  
Tomas D. Perez ◽  
W. James Nelson ◽  
Steven G. Boxer ◽  
Lance Kam
2007 ◽  
Vol 2 (4) ◽  
pp. 165-172 ◽  
Author(s):  
Rémi Bérat ◽  
Murielle Rémy-Zolghadry ◽  
Céline Gounou ◽  
Claude Manigand ◽  
Sisareuth Tan ◽  
...  

Soft Matter ◽  
2021 ◽  
Author(s):  
Long Li ◽  
Jie Gao ◽  
Yingfeng Shao ◽  
Fan Song ◽  
Jinglei Hu

The adhesion of cells to supported lipid bilayers (SLBs) has been widely used as model systems to study the receptor-ligand interactions that cause the membrane interface. The ligand-functionalized SLBs are...


2003 ◽  
Vol 64A (4) ◽  
pp. 622-629 ◽  
Author(s):  
Ann-Sofie Andersson ◽  
Karin Glasmästar ◽  
Duncan Sutherland ◽  
Ulf Lidberg ◽  
Bengt Kasemo

2010 ◽  
Vol 8 (7) ◽  
pp. 1531 ◽  
Author(s):  
Ludivine Sandrin ◽  
Liliane Coche-Guérente ◽  
Amandine Bernstein ◽  
Hajra Basit ◽  
Pierre Labbé ◽  
...  

2005 ◽  
Vol 173 (4S) ◽  
pp. 170-170
Author(s):  
Maxine G. Tran ◽  
Miguel A. Esteban ◽  
Peter D. Hill ◽  
Ashish Chandra ◽  
Tim S. O'Brien ◽  
...  

2018 ◽  
Author(s):  
Luke Jordan ◽  
Nathan Wittenberg

This is a comprehensive study of the effects of the four major brain gangliosides (GM1, GD1b, GD1a, and GT1b) on the adsorption and rupture of phospholipid vesicles on SiO2 surfaces for the formation of supported lipid bilayer (SLB) membranes. Using quartz crystal microbalance with dissipation monitoring (QCM-D) we show that gangliosides GD1a and GT1b significantly slow the SLB formation process, whereas GM1 and GD1b have smaller effects. This is likely due to the net ganglioside charge as well as the positions of acidic sugar groups on ganglioside glycan head groups. Data is included that shows calcium can accelerate the formation of ganglioside-rich SLBs. Using fluorescence recovery after photobleaching (FRAP) we also show that the presence of gangliosides significantly reduces lipid diffusion coefficients in SLBs in a concentration-dependent manner. Finally, using QCM-D and GD1a-rich SLB membranes we measure the binding kinetics of an anti-GD1a antibody that has similarities to a monoclonal antibody that is a hallmark of a variant of Guillain-Barre syndrome.


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