Lipid bilayer composition can influence the orientation of proteorhodopsin in artificial membranes.

Artificial membrane systems allow researchers to study the structure and function of membrane proteins in a matrix that approximates their natural environment and to integrate these proteins in ex vivo devices such as electronic biosensors, thin-film protein arrays, or biofuel cells. Given that most membrane proteins have vectorial functions, both functional studies and applications require effective control over protein orientation within a lipid bilayer. In this work, we explored the role of the bilayer surface charge in determining transmembrane protein orientation and functionality during formation of proteoliposomes. We reconstituted a model vectorial ion pump, proteorhodopsin, in liposomes of opposite charges and varying charge densities and determined the resultant protein orientation. Antibody-binding assay and proteolysis of proteoliposomes showed physical evidence of preferential orientation, and functional assays verified the vectorial nature of ion transport in this system. Our results indicate that the manipulation of lipid composition can indeed control orientation of an asymmetrically charged membrane protein, proteorhodopsin, in liposomes

Lipid bilayer composition can influence the orientation of proteorhodopsin in artificial membranes.

Artificial membrane systems allow researchers to study the structure and function of membrane proteins in a matrix that approximates their natural environment and to integrate these proteins in ex vivo devices such as electronic biosensors, thin-film protein arrays, or biofuel cells. Given that most membrane proteins have vectorial functions, both functional studies and applications require effective control over protein orientation within a lipid bilayer. In this work, we explored the role of the bilayer surface charge in determining transmembrane protein orientation and functionality during formation of proteoliposomes. We reconstituted a model vectorial ion pump, proteorhodopsin, in liposomes of opposite charges and varying charge densities and determined the resultant protein orientation. Antibody-binding assay and proteolysis of proteoliposomes showed physical evidence of preferential orientation, and functional assays verified the vectorial nature of ion transport in this system. Our results indicate that the manipulation of lipid composition can indeed control orientation of an asymmetrically charged membrane protein, proteorhodopsin, in liposomes

Electrochemically Grown Single Nanowire Sensors

We report a fabrication technique that is potentially capable of producing arrays of individually addressable nanowire sensors with controlled dimensions, positions, alignments, and chemical compositions. The concept has been demonstrated with electrodeposition of palladium wires with 75 nm to 350 nm widths. We have also fabricated single and double conducting polymer nanowires (polyaniline and polypyrrole) with 100nm and 200nm widths using electrochemical direct growth. Using single Pd nanowires, we have also demonstrated hydrogen sensing. It is envisioned that these are the first steps towards nanowire sensor arrays capable of simultaneously detecting multiple chemical species