Abstract
Cytoskeletal protein tubulin, when complexed with multi-walled carbon nanotubes (MWCN), was found to be able to direct various types of nanotube morphologies over different length scales. Rhodamine-labeled biotinylated tubulin was physically adsorbed onto the CNTs by incubating the protein with MWNTs for 2 hrs in Pipes-based buffer at 4°C with shaking at 200rpm. The results show patterns of Tubulin-MWNT conjugates in petal-like arrangements and these patterns form similar objects carrying similar edge effects. Sidewall-tubulin attachment promotes inter-MWNT interactions through nonselective hydrophobic protein-MWNT contacts, which lead to bundle formation in radial and axial dimensions. It is also found that in the absence of free tubulin in solution, polymerization of the high-loading tubulin-MWNT conjugates followed by Alexa-streptavidin staining results in undefined architectures.
Original language | English |
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Pages (from-to) | 310-315 |
Number of pages | 6 |
Journal | Small |
Volume | 5 |
Issue number | 3 |
DOIs | |
State | Published - 6 Feb 2009 |
Externally published | Yes |
Keywords
- Blomimetics
- Carbon nanotubes
- Encapsulation
- Self-assembly