Orientation and two-dimensional organization of proteins at chelator lipid interfaces

The analysis how proteins interact or assemble with each other in time and space is of central interest. Bio-functionalized interfaces can be applied to study protein-protein interactions in solution or elementary biological processes at membranes. Chelator lipid layers ave well suited for these applications as they specifically bind histidine-tagged fusion proteins and further mimic the two-dimensional world of biological membranes. Here, we used green fluorescent protein (GFP) as a model to study its reversible, functional, and oriented immobilization via histidine-tag at chelator lipid interfaces by various surface sensitive techniques. Taking advantage of the self-organizing properties of chelator lipids, the association and dissociation kinetics, the surface density as well as the organization of the protein in two-dimensional arrays can be controlled. The chelator lipid system can be used for bioanalytical and structural studies as well as to examine recognition processes at membranes.