AVS 57th International Symposium & Exhibition
    Nanometer-scale Science and Technology Thursday Sessions
       Session NS+BI-ThA

Invited Paper NS+BI-ThA6
Molecular Shuttles for 'Smart Dust' Biosensors, Active Self-Assembly, and Protein-Resistant Coatings

Thursday, October 21, 2010, 3:40 pm, Room La Cienega

Session: Biomolecular Templates & Bioinspired Nanomaterials
Presenter: H. Hess, Columbia University
Correspondent: Click to Email

Biomolecular motors, such as the motor protein kinesin, can serve as biological components in engineered nanosystems. Initially, a nanoscale transport system termed molecular shuttle has been explored by others and us as a model system. The development of this system has revealed a number of challenges in engineering at the nanoscale, particularly in the guiding, activation, and loading of these shuttles. Overcoming these challenges requires the integration of a diverse set of technologies, and continues to illustrate the complexity of biophysical mechanisms.

A proof-of-principle application of the developed technologies is a “smart dust” biosensor for the remote detection of biological and chemical agents, which is enabled by the integration of recognition, transport and detection into a submillimeter-sized microfabricated device.

The application of nanoscale forces introduces an interesting element into self-assembly processes by accelerating transport, reducing unwanted connections, and enabling the formation of non-equilibrium structures. The formation of nanowires and nanospools from microtubules transported by kinesin motors strikingly illustrates these aspects of motor-driven self-assembly.

Finally, a critical aspect of the design of these hybrid systems is the controlled adsorption of proteins. In pursuit of this goal of controlled adsorption, we have utilized kinesin motors as probes of residual protein adsorption to non-fouling coatings and achieved the detection of a few adsorbed molecules per square micrometer (adsorbed mass on the order of pg/cm2). Furthermore, we have developed a Random Sequential Adsorption model which successfully explains residual protein adsorption as the result of randomly occuring "bald" spots on a surface covered with PEG-chains.