Construction of artificial cilia from microtubules and kinesins through a well-designed bottom-up approach
Source abstract
Abstract
Self-organized structures of biomolecular motor systems, such as cilia and flagella, play key roles in the dynamic processes of living organisms, like locomotion or the transportation of materials. Although fabrication of such self-organized structures from reconstructed biomolecular motor systems has attracted much attention in recent years, a systematic construction methodology is still lacking. In this work, through a bottom-up approach, we fabricated artificial cilia from a reconstructed biomolecular motor system, microtubule/kinesin. The artificial cilia exhibited a beating motion upon the consumption, by the kinesins, of the chemical energy obtained from the hydrolysis of adenosine triphosphate (ATP). Several design parameters, such as the length of the microtubules, the density of the kinesins along the microtubules, the depletion force among the microtubules, etc., have been identified, which permit tuning of the beating frequency of the artificial cilia. The beating frequency of the artificial cilia increases upon increasing the length of the microtubules, but declines for the much longer microtubules. A high density of the kinesins along the microtubules is favorable for the beating motion of the cilia. The depletion force induced bundling of the microtubules accelerated the beating motion of the artificial cilia and increased the beating frequency. This work helps understand the role of self-assembled structures of the biomolecular motor systems in the dynamics of living organisms and is expected to expedite the development of artificial nanomachines, in which the biomolecular motors may serve as actuators.
Source: openalex_inverted_index · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Micro and Nano Robotics · Microtubule and mitosis dynamics · Genetic and Kidney Cyst Diseases
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Graduate School of Chemical Sciences and Engineering
Hokkaido University
Sapporo
Japan
Faculty of Science
Graduate School of Life Science
Department of Computational Intelligence and Systems Science
Tokyo Institute of Technology
Yokohama
Funding
Japan Society for the Promotion of Science
References (50)
Show source-provided references
1. J. Wang , in Nanomachines: fundamentals and applications , John Wiley & Sons , 201310.1002/9783527651450 ↗
2. Knoblauch · Cell. Mol. Life Sci. · 2004 · 61 · 19249710.1007/s00018-004-4158-0 ↗
3. Hess · Annu. Rev. Biomed. Eng. · 2011 · 13 · 42910.1146/annurev-bioeng-071910-124644 ↗
4. J. Howard , in Mechanics of motor proteins and the cytoskeleton , Sinauer Associates Inc. , 2001
5. J. Watson , B.Alberts , D.Bray , M.Raff and J.Lewis , in Molecular biology of the cell , Garland Science , 2007
6. Lam · Soft Matter · 2016 · 12 · 98810.1039/C5SM02042E ↗
7. Hess · Chem. Soc. Rev. · 2017 · 46 · 557010.1039/C7CS00030H ↗
8. Ndlec · Nature · 1997 · 389 · 30510.1038/38532 ↗
9. Ohba · Science · 1999 · 284 · 135610.1126/science.284.5418.1356 ↗
10. Sumino · Nature · 2012 · 483 · 44810.1038/nature10874 ↗
11. Suzuki · Proc. Natl. Acad. Sci. U. S. A. · 2017 · 201616001
12. Hess · Nano Lett. · 2005 · 5 · 62910.1021/nl0478427 ↗
13. Keya · Nat. Commun. · 2018 · 9 · 45310.1038/s41467-017-02778-5 ↗
14. Tamura · Soft Matter · 2011 · 7 · 565410.1039/c1sm05413a ↗
15. Kawamura · Langmuir · 2009 · 26 · 53310.1021/la902197f ↗
16. Sanchez · Science · 2011 · 333 · 45610.1126/science.1203963 ↗
17. Cobo · Nat. Mater. · 2015 · 14 · 14310.1038/nmat4106 ↗
18. Castoldi · Protein Expression Purif. · 2003 · 32 · 8310.1016/S1046-5928(03)00218-3 ↗
19. Case · Cell · 1997 · 90 · 95910.1016/S0092-8674(00)80360-8 ↗
20. Peloquin · Nat. Methods · 2005 · 2 · 29910.1038/nmeth0405-299 ↗
21. Inoue · Nanoscale · 2015 · 7 · 1805410.1039/C5NR02213D ↗
22. Orihara · Phys. Rev. E: Stat., Nonlinear, Soft Matter Phys. · 2011 · 83 · 02630210.1103/PhysRevE.83.026302 ↗
23. Saito · RSC Adv. · 2017 · 7 · 1319110.1039/C6RA27449H ↗
24. Satir · J. Cell Biol. · 1968 · 39 · 7710.1083/jcb.39.1.77 ↗
25. Summers · Proc. Natl. Acad. Sci. U. S. A. · 1971 · 68 · 309210.1073/pnas.68.12.3092 ↗
26. Kobayashi · Macromolecules · 1999 · 32 · 707010.1021/ma990242n ↗
27. Niggemann · Eur. J. Pediatr. · 1992 · 151 · 7310.1007/BF02073899 ↗
28. Pazour · J. Cell Biol. · 2005 · 170 · 10310.1083/jcb.200504008 ↗
29. Gibbons · J. Cell Biol. · 1972 · 74 · 7510.1083/jcb.54.1.75 ↗
30. Heuser · J. Cell Biol. · 2009 · 187 · 92110.1083/jcb.200908067 ↗
31. Minoura · Cell Struct. Funct. · 1999 · 24 · 2710.1247/csf.24.27 ↗
32. Lau · EPL · 2009 · 87 · 4800610.1209/0295-5075/87/48006 ↗
33. Claessens · Nat. Mater. · 2006 · 5 · 74810.1038/nmat1718 ↗
34. Gibbons · J. Cell Biol. · 1981 · 91 · 107s10.1083/jcb.91.3.107s ↗
35. Gadelha · Cell Motil. Cytoskeleton · 2007 · 64 · 62910.1002/cm.20210 ↗
36. Vandecandelaere · Biochemistry · 1995 · 34 · 133210.1021/bi00004a028 ↗
37. Ray · J. Cell Biol. · 1993 · 121 · 108310.1083/jcb.121.5.1083 ↗
38. Buceta · Biophys. J. · 2005 · 89 · 219910.1529/biophysj.105.063743 ↗
39. McGrath · Cell · 2003 · 114 · 6110.1016/S0092-8674(03)00511-7 ↗
40. Satir · J. Cell Sci. · 2010 · 123 · 49910.1242/jcs.050377 ↗
41. Jülicher · Phys. Rev. Lett. · 1997 · 78 · 451010.1103/PhysRevLett.78.4510 ↗
42. Camalet · Phys. Rev. Lett. · 1999 · 82 · 159010.1103/PhysRevLett.82.1590 ↗
43. Placais · Phys. Rev. Lett. · 2009 · 103 · 15810210.1103/PhysRevLett.103.158102 ↗
44. Guérin · Curr. Opin. Cell Biol. · 2010 · 22 · 1410.1016/j.ceb.2009.12.012 ↗
45. Gittes · Biophys. J. · 1996 · 70 · 41810.1016/S0006-3495(96)79585-1 ↗
46. Brangwyne · Phys. Rev. Lett. · 2008 · 100 · 11810410.1103/PhysRevLett.100.118104 ↗
47. van-den-Heuvel · Science · 2006 · 312 · 91010.1126/science.1124258 ↗
48. Agarwal · Prog. Polym. Sci. · 2010 · 35 · 25210.1016/j.progpolymsci.2009.10.007 ↗
49. Limberis · Nanotechnology · 2000 · 11 · 4710.1088/0957-4484/11/2/301 ↗
50. Hess · Chem. – Eur. J. · 2004 · 10 · 211010.1002/chem.200305712 ↗