Cavity Control of Prefoldin Nano Actuator (PNA) by Temperature and pH
Corresponding Author: Reza Hasanzadeh Ghasemi
Nano-Micro Letters,
Vol. 4 No. 2 (2012), Article Number: 110-117
Abstract
A molecular dynamics study to investigate the cavity control of Prefoldin based bio nano actuator is presented in this paper. Prefoldin is a molecular chaperone with a jellyfish-like structure containing six long coiled-coil tentacles and a large central cavity. We took the temperature and pH of the medium into account, and analyzed the conformational flexibility of the Prefoldin nano actuator in details. Results show that the prefoldin is a very flexible protein, the conformational state of which appears to depend on the temperature and pH values of the medium. In fact, combining these two control parameters, a suitable environment is provided to capture nano cargoes with specific dimensions. These properties of Prefoldin actuator can be used for drug delivery in the body.
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- G. Sharma, K. Rege, C. Mavroidis and M. L. Yarmush, “Design and Modeling of a Peptide Based Nanotweezer”, ASME International Design Engineering Technical Conferences, Philadelphia, Pennsylvania, USA, 2006.
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- S. Geissler, K. Siegers and E. Schiebel, EMBO J. 17, 952 (1998). http://dx.doi.org/10.1093/emboj/17.4.952
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References
G. Sharma, K. Rege, C. Mavroidis and M. L. Yarmush, “Design and Modeling of a Peptide Based Nanotweezer”, ASME International Design Engineering Technical Conferences, Philadelphia, Pennsylvania, USA, 2006.
A. Dubey, G. Sharma, C. Mavroidis, M. S. Tomassone, K. Nikitczuk and M. L. Yarmush, J. Comput. Theor. Nanosci. 1, 18 (2004). http://dx.doi.org/10.1166/jctn.2003.003
A. Dubey, C. Mavroidis and M. S. Tomassone, J. Comput. Theor. Nanosci. 3, 885 (2006). http://dx.doi.org/10.1166/jctn.2006.005
G. S. Chirikjian, K. Kazerounian and C. Mavroidis, J. Mech. Design 127, 695 (2005). http://dx.doi.org/10.1115/1.1901706
A. Dubey, G. Sharma, C. Mavroidis, S. M. Tomassone, K. Nikitczuk and M. L. Yarmush, “Dynamics and Kinematics of Viral Protein Linear Nano-Actuators for Bio-Nano Robotic Systems”, Proceedings of the IEEE, International Conference on Robotics & Automation, New Orleans, LA, April 2004.
G. Sharma, M. Badescu, A. Dubey, C. Mavroidis, S. M. Tomassone and M. L. Yarmush, Transactions of the ASME 127, 718 (2005). http://dx.doi.org/10.1115/1.1900751
M. Hamdi, A. Ferreira, G. Sharma and C. Mavroidis, Microelectronics J. 39, 190 (2008). http://dx.doi.org/10.1016/j.mejo.2006.12.003
A. Ghaffari, A. Shokuhfar and R. Hasanzadeh Ghasemi, J. Comput. Theor. Nanosci. 8, 2406 (2011). http://dx.doi.org/10.1166/jctn.2011.1929
S. Geissler, K. Siegers and E. Schiebel, EMBO J. 17, 952 (1998). http://dx.doi.org/10.1093/emboj/17.4.952
I. E. Vainberg, S. A. Lewis, H. Rommelaere, C. Ampe, J. Vandekerckhove, H. L. Klein and N. J. Cowan, Cell 93, 863 (1998). http://dx.doi.org/10.1016/S0092-8674(00)81446-4
T. Zako, Y. Murase, R. Iizuka, T. Yoshida, T. Kanzaki and N. Ide, J. Mol. Biol. 364, 110 (2006). http://dx.doi.org/10.1016/j.jmb.2006.08.088
http://en.wikipedia.org/wiki/Prefoldin
A. Pockley, Molecular Chaperones and Cell Signaling, Cambridge University Press, Cambridge 2005.
J. Martin-Benito, J. Gomez-Reino, P. C. Stirling, V. F. Lundin, P. Gomez-Puertas and J. Boskovic, Structure 15, 101 (2007). http://dx.doi.org/10.1016/j.str.2006.11.006
A. Ghaffari, A. Shokuhfar and R. Hasanzadeh Ghasemi, “Characterization of Prefoldin Based Nano Gripper”, International Congress on Nanoscience and Nanotechnology, Shiraz, Iran, 2010.
A. Ghaffari, R. Hasanzadeh Ghasemi and A. Shokuhfar, “Molecular Dynamics Studies of a Novel Nano Actuator Based on Archaeal Prefoldin”, The 17th Iranian Conference on Biomedical Engineering, Isfahan, Iran, 2010.
A. Ghaffari, A. Shokuhfar, R. Hasanzadeh Ghasemi, “Design and Simulation of a Novel Bio Nano Actuator by Prefoldin”, IEEE Nano Conference, Seoul, South Korea, 2010. http://dx.doi.org/10.1109/NANO.2010.5697837
A. Ohtaki, H. Kida, Y. Miyata, N. Ide, A. Yonezawa, T. Arakawa, R. Iizuka, K. Noguchi, A. Kita, M. Odaka, K. Miki and M. Yohda, J. Mol. Biol. 376, 1130 (2008). http://dx.doi.org/10.1016/j.jmb.2007.12.010
T. Zako, R. Iizuka, M. Okochi, T. Nomura, T. Ueno and H. Tadakuma, FEBS Lett. 579, 3718 (2005). http://dx.doi.org/10.1016/j.febslet.2005.05.061
R. Siegert, M. R. Leroux, C. Scheufler, F. U. Hartl and I. Moarefi, Cell 103, 621 (2000). http://dx.doi.org/10.1016/S0092-8674(00)00165-3
R. Iizuka, Y. Sugano, N. Ide, A. Ohtaki, T. Yoshida, S. Fujiwara, T. Imanaka and M. Yohda, J. Mol. Biol. 377, 972 (2008). http://dx.doi.org/10.1016/j.jmb.2008.01.070
H. M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T. N. Bhat, H. Weissig, I. N. Shindyalov and P. E. Bourne, Nucleic Acids Res. 28, 235 (2000). http://dx.doi.org/10.1093/nar/28.1.235
H. Li, A. D. Robertson and J. H. Jensen, Proteins 61, 704 (2005). http://dx.doi.org/10.1002/prot.20660