Assembly and molecular organization of self-assembled lipid bilayers on solid substrates monitored by surface plasmon resonance spectroscopy

1994 ◽  
Vol 1195 (2) ◽  
pp. 267-275 ◽  
Author(s):  
Zdzislaw Salamon ◽  
Yin Wang ◽  
Gordon Tollin ◽  
H.Angus Macleod
2001 ◽  
Vol 50 (2) ◽  
pp. 109-115 ◽  
Author(s):  
Sung-Hoon Kim ◽  
Sung-Wook Choi ◽  
Jae-Ho Kim ◽  
Sung-Ho Jin ◽  
Yeong-Soon Gal ◽  
...  

2002 ◽  
Vol 16 (3-4) ◽  
pp. 271-279 ◽  
Author(s):  
Torsten Fischer ◽  
Ivan I. Senin ◽  
Pavel P. Philippov ◽  
Karl-Wilhelm Koch

Planar lipid bilayers on sensor chip surfaces have become useful tools to study membrane bound processes by surface plasmon resonance spectroscopy. We immobilized phospholipids on sensor chips by different approaches. First, a self-assembled monolayer of octadecylmercaptan was formed on a blank gold surface and subsequent addition of phospholipids led to formation of a heterobilayer. Second, a self-assembled monolayer of mercaptoundecanoic acid was formed on a gold surface, the carboxy groups of mercaptoundecanoic acid were activated and covalently linked to phosphatidylethanolamine. Addition of phospholipids then led to a bilayer with phosphatidylethanolamine as the lower leaflet. Third, a hydrophobic sensor chip (L1, BIAcore) was used as a binding matrix for phospholipids. These lipid surfaces were tested, whether they are suitable to study proteinamembrane interactions. As biological test system we used the Ca2+-myristoyl-switch of the neuronal Ca2+-binding protein recoverin. All three surfaces were sufficiently stable to monitor the Ca2+-dependent binding of recoverin to membranes.


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