Abstract
The β-lactoglobulin (β-LG) protein was discovered to be an efficient and selective dispersant for carbon nanotubes (CTNs) with certain diameters. A dispersion process of CTNs by the β-LG was studied, focusing on the relationships between the surface curvature of the CNT and the β-LG's efficiency in dispersing them, using cryogenic-transmission electron microscopy (cryo-TEM) and optical spectroscopy. Plausible binding sites of the β-LG, responsible for the interaction of the protein with CNTs of various diameters (surface curvatures) were also investigated and were found to be in good agreement with corresponding docking calculations.
Original language | English |
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Pages (from-to) | 16-22 |
Number of pages | 7 |
Journal | Colloids and Surfaces B: Biointerfaces |
Volume | 112 |
DOIs | |
State | Published - 1 Dec 2013 |
Keywords
- Carbon nanotubes
- Cryo-TEM
- Dispersion
- Docking
- Surface curvature
All Science Journal Classification (ASJC) codes
- Biotechnology
- Surfaces and Interfaces
- Physical and Theoretical Chemistry
- Colloid and Surface Chemistry