Journal of Spectroscopy

Journal of Spectroscopy / 2002 / Article

Open Access

Volume 16 |Article ID 630549 |

Torsten Fischer, Ivan I. Senin, Pavel P. Philippov, Karl-Wilhelm Koch, "Application of Different Lipid Surfaces to Monitor Protein–Membrane Interactions by Surface Plasmon Resonance Spectroscopy", Journal of Spectroscopy, vol. 16, Article ID 630549, 9 pages, 2002.

Application of Different Lipid Surfaces to Monitor Protein–Membrane Interactions by Surface Plasmon Resonance Spectroscopy


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.

Copyright © 2002 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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