Molecular and Nanometer-Scale Self-Organized System Generated by Protein Motor Functions


Article Preview

Creatures have evolved extremely intelligent and complex adaptive systems for conducting their movements. They are protein motors with typical sizes of a few tens of nanometers. Protein motors include three major protein families, myosin, kinesin and dynein, which participate in a wide range of cellular processes, using energy from the hydrolysis of adenosinetriphosphate ATP. To harness these protein motors to power nanometer-scale devices, we have investigated effective and non-destructive methods for immobilizing protein motors on surfaces and to arrange the output of these motors, e.g. force and movement, to be in a defined direction. We found NEB-22 to be useful for retaining the abilities of protein motors to support the movement of protein filaments. We fabricated various patterns of tracks of NEB-22 on coverslips and protein motors were introduced and immobilized on glass surface. The trajectories of protein polymers were confined to these tracks. Simple patterns readily biased and guide polymer movement confining it to be unidirectional. In addition, having used dynein c purified from Chlamydomonas flagellar axoneme, we showed that microtubules driven by surface-bound dynein were self-organized into dynamic streams through collisions between the microtubules and their subsequent joining.



Materials Science Forum (Volumes 539-543)

Main Theme:

Edited by:

T. Chandra, K. Tsuzaki, M. Militzer , C. Ravindran




K. Oiwa et al., "Molecular and Nanometer-Scale Self-Organized System Generated by Protein Motor Functions", Materials Science Forum, Vols. 539-543, pp. 3290-3296, 2007

Online since:

March 2007




[1] K. Oiwa and H. Sakakibara: Curr. Opin. Cell Biol. 17 (2005), 98-103.

[2] H. Sakakibara, H. Kojima, Y. Sakai, E. Katayama, and K. Oiwa: Nature 400 (1999), 586-590.


[3] A. Hyman, D. Drechsel, D. Kellogg, S. Salser, K. Sawin, P. Steffen, L. Wordeman, and T. Mitchison: Methods Enzymol. 196 (1991), 478-485.


[4] Y. Hiratsuka, T. Tada, K. Oiwa, T. Kanayama, and T.Q. Uyeda: Biophys. J. 81 (2001), 1555-1561.

[5] H. Suzuki, A. Yamada, K. Oiwa, H. Nakayama, and S. Mashiko: Biophys. J. 72 (1997), 1997-(2001).

[6] M. G. L. van den Heuvel, C. T. Butcher, R. M. M. Smeets, S. Diez, and C. Dekker: Nano Letters 5 (2005), 1117-1122.

[7] D. C. Turner, C. Chang, K. Fang, S. L. Brandow, and D. B. Murphy: Biophys. J. 69 (1995), 2782-2789 8. H. Suzuki, K. Oiwa, A. Yamada, H. Sakakibara, H. Nakayama, and S. Mashiko: Japan. J. Appl. Phys. 34 (1995), 3937-3941.

[9] D. V. Nicolau, H. Suzuki, S. Mashiko, T. Taguchi, and S. Yoshikawa: Biophys. J. 77 (1999), 1126-1134.

[10] J. Clemmens, H. Hess, J. Howard, and V. Vogel: Langmuir 19 (2003), 1738-1744.

[11] J. Clemmens, H. Hess, R. Lipscomb, Y. Hanein, K.F. Bohringer, C.M. Matzke, G.D. Bachand, B.C. Bunker, and V. Vogel: Langmuir 19 (2003), 10967-10974.


[12] R. Bunk, M. Sundberg, A. Mansson, I.A. Nicholls, P. Omling, S. Tagerud, and L. Montelius: Nanotechnology 16 (2005), 710-717.


[13] J. H. Kaplan: J. Gen. Physiol. 84 (1984), A9-A10.

[14] J. A. Mccray, L. Herbette, T. Kihara, and D.R. Trentham: Proc. Natl. Acad. Sci. U. S A 77 (1980), 7237-7241.

[15] G. Marriott, P. Roy, and K. Jacobson: Methods Enzymol. 360 (2003), 274-288.

[16] G. Marriott, and M. Heidecker: Biochemistry 35 (1996), 3170-3174.