Electroless metal plating of microtubules: Effect of microtubule-associated proteins
Source abstract
Abstract
Microtubules (MTs) are self-assembled proteinaceous filaments with nanometer scale diameters and micrometer scale lengths. Their aspect ratio, the reversibility of their assembly and their ability to be metallized by electroless plating make them good candidates to serve as templates for the fabrication of nanowires. We have shown that microtubule-associated-proteins (MAPs) play a critical role in maintaining the MT stability during Pt-catalyzed electroless Ni plating. MAP-stabilized MTs metallized for one minute in a Ni-acetate-based electroless-plating bath are coated with a metal film only several nanometers thick. The MAPs appear to lead to the formation of nanometer-wide metal bridges between the MTs. The metal coatings are constituted of small Pt clusters (∼3 nm), distributed and oriented randomly, embedded in an amorphous nickel matrix.
Source: openaire · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Microtubule and mitosis dynamics · Molecular Junctions and Nanostructures · Photosynthetic Processes and Mechanisms
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (23)
Show source-provided references
1. N. C. Seeman and A. M. Belcher, PNAS 99 (2002) 6451.10.1073/pnas.221458298 ↗
2. C. A. Mirkin, Mater. Res. Soc. Bull. 25 (2000) 43.10.1557/S0883769400065015 ↗
3. A. P. Alivisatos, K. P. Johnsson, X. G. Peng, T. E. Wilson, C. J. Loweth, M. B. Bruchez and P. G. Schultz, Nature 382 (1996) 609.10.1038/382609a0 ↗
4. J. K. N. Mirbindyo, B. D. Resis, B. R. Martin, C. D. Keating, M. J. Natan and T. E. Mallouk, Adv. Mater. 13 (2001) 249.10.1002/1521-4095(200102)13:4<249::AID-ADMA249>3.0.CO;2-9 ↗
5. E. Braun, Y. Eichen, U. Sivan and G. Benyoseph, Nature 391 (1998) 775.10.1038/35826 ↗
6. S. Vauthey, S. Santoso, H. Gong, N. Watson and S. Zhang, PNAS 99 (2002) 5355.10.1073/pnas.072089599 ↗
7. G. E. Douberly, S. Pan, D. Walters and H. Matsui, J. Phys. Chem. B 105 (2001) 7621.10.1021/jp0102217 ↗
8. H. Matsui, P. Porrata and G. E. Douberly, Nano Lett. 1 (2001) 461.10.1021/nl015564v ↗
9. G. M. Chow, M. Pazirandeh, S. Baral and J. R. Campbell, Nano-Struct. Mater. 2 (1993) 495.10.1016/0965-9773(93)90167-A ↗
10. T. Scheibel, R. Parthasarathy, G. Sawicki, X. Lin, H. M. Jaeger and S. L. Lindquist, Proc. Natl. Acad. Sci. USA 100 (2003) 4527.10.1073/pnas.0431081100 ↗
11. M. Mertig, R. Kirsch and W. Pompe, Appl. Phys. A 66 (1998) S723.10.1007/s003390051230 ↗
12. K. Kinoshita, I. Arnal, A. Desai, D. N. Drechsel and A. A. Hyman, Science 294 (2001) 1340.10.1126/science.1064629 ↗
13. S. Behrens, K. Rahn, N. Habicht, K. J. Bohm, H. Rosner, E. Dinjus and E. Unger, Adv. Mater. 14(22) (2002) 1621.10.1002/1521-4095(20021118)14:22<1621::AID-ADMA1621>3.0.CO;2-D ↗
14. R. Kirsch, M. Mertig, W. Pompe, R. Wahl, G. Sadowski, K. J. Bohm and E. Unger, Thin Solid Films 305 (1997) 248.10.1016/S0040-6090(97)00131-4 ↗
15. S. C. Schuyler and D. Pellman, Cell. 105(4) (2001) 421.10.1016/S0092-8674(01)00364-6 ↗
16. M. J. Schilstra, P. M. Bayley and S. R. Martin, Biochem. J. 227 (1991) 839.10.1042/bj2770839 ↗
17. L. A. Amos and L. Jan, Chem. Biol. 6 (1999) 65.10.1016/S1074-5521(99)89002-4 ↗
18. I. Arnal and R. H. Wade, Curr. Biol. 5 (1995) 900.10.1016/S0960-9822(95)00180-1 ↗
19. A. Desai and T. J. Mitchison, Annu. Rev. Cell Dev. Biol. 13 (1997) 83.10.1146/annurev.cellbio.13.1.83 ↗
20. H. Felgner, R. Frank, J. Biernat, E. M. Mandelkow, E. Mandelkow, B. Ludin, A. Matus and M. Schliwa, J. Cell. Biol. 138 (1997) 1067.10.1083/jcb.138.5.1067 ↗
21. E. Hamel, A. A. Delcampo, M. Lowe and C. M. Lin, J. Biol. Chem. 256 (1981) 11887.10.1016/S0021-9258(19)68489-9 ↗
22. T. S. Ahmadi, Z. L. Wang, T. C. Green, A. Henglein and M. A. El-Sayed, Science 272 (1997) 1924.10.1126/science.272.5270.1924 ↗
23. L. C. Ciacchi, P. Wolfgang and D. V. Alessandro, J. Amer. Chem. Soc. 123 (2001) 7371.10.1021/ja002977+ ↗