Attachment of motor proteins to thiol monolayers on gold surfaces

COLL 186

Hernesto Tellez1, Andrew K. Boal2, Susan B. Rivera2, George D. Bachand2, and Bruce C. Bunker2. (1) Biomolecular Materials and Interfaces, Sandia National Labs, PO BOX 5800, Albuquerque, NM 87102, (2) Biomolecular Materials and Interfaces, Sandia National Laboratories, BOX 5800, Albuquerque, NM 87123
Our current research focuses on the integration of the microtubules (MTs) and motor protein kinesin into microfluidic devices for the purposes of developing active nanomaterials assembly systems. One of the key areas of this research is to develop an understanding of the interface between synthetic surfaces and motor proteins. To accomplish this, we have prepared a series of alkane thiol self-assembled monolayers displaying numerous functional groups on gold surfaces. To study interactions with MTs, these surfaces were exposed to a solution of MTs and interrogated using florescence microscopy to determine the relative binding affinity of the MTs to the surface. In the case of kinesin, surfaces were first exposed to kinesin and then MTs. Upon observation of these surfaces under the microscope, we could not only determine which surfaces bind kinesin, but also confirm that the kinesin activity by observing the MTs gliding across the surface.