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 |
|---|---|
| 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
ASJC Scopus subject areas
- Biotechnology
- Surfaces and Interfaces
- Physical and Theoretical Chemistry
- Colloid and Surface Chemistry