Research Overview

Sophisticated nanomotors have evolved in nature, where motor proteins actively control the delivery and assembly of materials within cells, and generate large forces by acting in arrays, for example in muscles. In contrast, the development of synthetic nanomotors is in its infancy.

We have successfully utilized motor proteins in synthetic environments for the controlled transport of nanoscale cargo, and continue to advance the design of such hybrid bionanodevices and –materials.

The hybrid approach has the advantage that techniques, materials and devices unique to either biology or technology can be merged into a revolutionary combination. Applications particularly suited to hybrid systems are found in medicine and biotechnology, where biocompatibility is critical and the environmental conditions are favorable for biological nanomachines.

Many technological applications however require temperature stability and durability beyond the limitations of biological components. Here hybrid devices can provide a proof-of-concept, but the challenge is to assemble synthetic nanomotors based on the biological design concepts which operate over a wide range of conditions.

Ultimately, working with individual or arrays of nanoscale motors requires a complete rethinking of engineering approaches to force generation and mass transport, including problems of control, efficiency, and scaling. Our goal is to realize the nanorevolution in this particular technology arena.

Energy Conversion  

In a combustion engine, chemical energy is first converted to heat to cause the expansion of a fluid which then produces motion. In contrast, motor proteins are molecules that can convert the chemical energy released from adenosine triphosphate (ATP) hydrolysis directly into useful mechanical work. For this reason, motor proteins are attractive solutions as the underlying force-generating structures of a potentially more efficient molecular engine. Our goal is to realize such a device by spatially organizing biomolecular motors from the bottom-up to create large-scale functional arrays capable of generating a macroscopic force output. Future developments include applications such as prosthetic and implantable actuators for biomedicine and force transducers for transport systems.


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Active self-assembly  

Transport and assembly of materials in biological systems is conducted at multiple scales, from the molecular level to whole organisms. With increasing size of building blocks, the assembly of complex, highly functional structures comes at a cost of reduced stability, since unintended connection must be weak in order to maintain sufficient yield. In order to overcome this drawback, nature employs biomolecular motors to assemble functional architectures with specific mechanical and optical properties from large building blocks. For example, the mitotic spindle consists of dozens of oriented microtubules arranged into an aster-like shape by motor proteins. Our work aims to formulate the rules governing these active self-assembly processes, and to show that the boundaries of self assembly can be greatly expanded by use of biomolecular motors.


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Wear  

Annual expenses due to friction and wear across the U.S. economy run up to hundreds of billions of dollars. To respond to this macroscopic problem, reliability research is an active area that aims at a better understanding of tribological interactions (friction, adhesion, and wear). Active biological nanomachines are also subject to friction and wear. Providing a mechanical understanding of those nanoscale phenomena is critical in securing the future of nanotechnology.


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Non-fouling surfaces  
Nonfouling

The suppression of protein adsorption to surfaces is a central challenge in biomedical engineering. When proteins acting as disease markers are adsorbed by the tubing of a biosensor, the signal is compromised. When blood proteins interact with the surface of an implant, the coagulation cascade is activated and a thrombus forms, which can have devastating consequences. The development of polymeric coatings, often based on poly(ethylene oxide), has made significant progress, but our ability to measure protein adsorption and our theoretical understanding have not kept up. Our work aims to advance characterization and theoretical understanding, so that chemists can further improve protein-resistant coatings.

 


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