Abstract
Eukaryotic cells use cytoskeletal tracks known as microtubules and motor proteins such as kinesin for transporting intracellular cargo and for positioning organelles. Kinesin motors move unidirectionally along microtubules using the energy from hydrolysis of adenosine triphosphate (ATP). Studies have shown that the forces generated by the kinesin motors are sufficient to mobilize synthetic devices. A critical component in realizing useful work from the directional motion of biomolecular motor protein systems involves patterning kinesin motors in pre-defined areas and aligning microtubules on various surfaces. In order to reduce another degree of freedom in such systems both kinesin and microtubules need to be patterned simultaneously. Traditional device fabrication processes such as lithography, however, are not considered compatible with the biological proteins. Accordingly in previous studies devices were fabricated first and functional proteins immobilized on them subsequently. To create hybrid biological and synthetic systems it may be necessary to integrate biological entities such as proteins with device fabrication processes. Toward this end, a series of experiments were conducted to investigate the compatibility of neutravidin and biotinylated kinesin with acetone, remover of electron beam resist poly methyl methacrylate (PMMA). It is found that neutravidin and biotinylated kinesin retain their functionality after acetone exposure. It is also found that exposure to PMMA does not defunctionalize. These studies open up a new approach for the micro and nanoscale patterning of biological molecular motors.
| Original language | English (US) |
|---|---|
| Title of host publication | Proceedings - 2005 International Symposium on Microelectronics, IMAPS 2005 |
| Pages | 244-249 |
| Number of pages | 6 |
| State | Published - Dec 1 2005 |
| Event | 38th International Symposium on Microelectronics, IMAPS 2005 - Philadelphia, PA, United States Duration: Sep 25 2005 → Sep 29 2005 |
Publication series
| Name | Proceedings - 2005 International Symposium on Microelectronics, IMAPS 2005 |
|---|
Other
| Other | 38th International Symposium on Microelectronics, IMAPS 2005 |
|---|---|
| Country | United States |
| City | Philadelphia, PA |
| Period | 9/25/05 → 9/29/05 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Electrical and Electronic Engineering
Cite this
}
Approaches for hybrid biological and synthetic system integration. / Verma, Vivek; Hancock, William O.; Catchmark, Jeffrey M.
Proceedings - 2005 International Symposium on Microelectronics, IMAPS 2005. 2005. p. 244-249 (Proceedings - 2005 International Symposium on Microelectronics, IMAPS 2005).Research output: Chapter in Book/Report/Conference proceeding › Conference contribution
TY - GEN
T1 - Approaches for hybrid biological and synthetic system integration
AU - Verma, Vivek
AU - Hancock, William O.
AU - Catchmark, Jeffrey M.
PY - 2005/12/1
Y1 - 2005/12/1
N2 - Eukaryotic cells use cytoskeletal tracks known as microtubules and motor proteins such as kinesin for transporting intracellular cargo and for positioning organelles. Kinesin motors move unidirectionally along microtubules using the energy from hydrolysis of adenosine triphosphate (ATP). Studies have shown that the forces generated by the kinesin motors are sufficient to mobilize synthetic devices. A critical component in realizing useful work from the directional motion of biomolecular motor protein systems involves patterning kinesin motors in pre-defined areas and aligning microtubules on various surfaces. In order to reduce another degree of freedom in such systems both kinesin and microtubules need to be patterned simultaneously. Traditional device fabrication processes such as lithography, however, are not considered compatible with the biological proteins. Accordingly in previous studies devices were fabricated first and functional proteins immobilized on them subsequently. To create hybrid biological and synthetic systems it may be necessary to integrate biological entities such as proteins with device fabrication processes. Toward this end, a series of experiments were conducted to investigate the compatibility of neutravidin and biotinylated kinesin with acetone, remover of electron beam resist poly methyl methacrylate (PMMA). It is found that neutravidin and biotinylated kinesin retain their functionality after acetone exposure. It is also found that exposure to PMMA does not defunctionalize. These studies open up a new approach for the micro and nanoscale patterning of biological molecular motors.
AB - Eukaryotic cells use cytoskeletal tracks known as microtubules and motor proteins such as kinesin for transporting intracellular cargo and for positioning organelles. Kinesin motors move unidirectionally along microtubules using the energy from hydrolysis of adenosine triphosphate (ATP). Studies have shown that the forces generated by the kinesin motors are sufficient to mobilize synthetic devices. A critical component in realizing useful work from the directional motion of biomolecular motor protein systems involves patterning kinesin motors in pre-defined areas and aligning microtubules on various surfaces. In order to reduce another degree of freedom in such systems both kinesin and microtubules need to be patterned simultaneously. Traditional device fabrication processes such as lithography, however, are not considered compatible with the biological proteins. Accordingly in previous studies devices were fabricated first and functional proteins immobilized on them subsequently. To create hybrid biological and synthetic systems it may be necessary to integrate biological entities such as proteins with device fabrication processes. Toward this end, a series of experiments were conducted to investigate the compatibility of neutravidin and biotinylated kinesin with acetone, remover of electron beam resist poly methyl methacrylate (PMMA). It is found that neutravidin and biotinylated kinesin retain their functionality after acetone exposure. It is also found that exposure to PMMA does not defunctionalize. These studies open up a new approach for the micro and nanoscale patterning of biological molecular motors.
UR - http://www.scopus.com/inward/record.url?scp=84876919184&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84876919184&partnerID=8YFLogxK
M3 - Conference contribution
AN - SCOPUS:84876919184
SN - 0930815777
SN - 9780930815776
T3 - Proceedings - 2005 International Symposium on Microelectronics, IMAPS 2005
SP - 244
EP - 249
BT - Proceedings - 2005 International Symposium on Microelectronics, IMAPS 2005
ER -