LOT-Oriel - Immobilization protocols

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Immobilization protocols

To be able to study for example protein interaction in a good way, suitable immobilization protocols are required. The immobilized protein should keep its native functions and unspecific binding should be avoided. Below some examples of suitable immobilization strategies for QCM-D. For the full version of these protocols please contact q-sense@lot-oriel.de.

		Supported lipid bilayer containing NTA/Ni2+ The obtained NTA/Ni-doped lipid bilayer is available for protein interactions via the unoccupancies on the Ni2+ ion. It has been shown that the amino acid Histidine has a certain affinity to the NTA/Ni complex, especially when appearing as an oligo-histidine with 6 residues in a row. Further methods for anchoring of proteins via His-tags can be found elsewhere. Non-functionalized supported lipid bilayers are found to be resistant to protein adsorption, which means that this immobilization approach is excellent for controlled immobilization and coupling events.

		Streptavidin coupled to Biotinized Phospholipid Bilayer The Streptavidin layer is available for interactions via further biotin coupling. Since non-functionalized supported lipid bilayers are found to be very resistant to protein adsorption, the surface is an excellent platform for controlled immobilization and coupling events. References include 'Characterization of PNA and DNA immobilization and subsequent hybridization with DNA using acoustic-shear-wave attenuation measurements' by Höök et al.

		Albumin-biotin and subsequent Streptavidin adsorption The obtained Streptavidin/Neutravidin layer in the panel to the left is suitable for immobilization of molecules via further biotin coupling. It should be noted that the inertness of biotinylated Albumin may not be as reliable as that of phospholipid bilayers. As to what Q-Sense knows, unspecific binding of molecules directly to free spots on the solid surface may occur in the next measurement step.

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