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Bioengineering, Food, and Natural Products
Protein adsorption on functionalized multiwalled carbon nanotubes with amino-cyclodextrin
Article first published online: 28 FEB 2011
DOI: 10.1002/aic.12543
Copyright © 2011 American Institute of Chemical Engineers (AIChE)
Additional Information
How to Cite
Li, L., Feng, W. and Ji, P. (2011), Protein adsorption on functionalized multiwalled carbon nanotubes with amino-cyclodextrin. AIChE J., 57: 3507–3513. doi: 10.1002/aic.12543
Publication History
- Issue published online: 4 NOV 2011
- Article first published online: 28 FEB 2011
- Accepted manuscript online: 7 JAN 2011 12:02PM EST
- Manuscript Revised: 4 JAN 2011
- Manuscript Received: 30 JUL 2010
Funded by
- National Science Foundation of China. Grant Numbers: 21076018, 20636010
- National Basic Research Program of China. Grant Numbers: 2007CB714302, 2011CB200905
- 863 Program. Grant Number: 2009AA033001
- Program for New Century Excellent Talents in University
- Abstract
- Article
- References
- Cited By
Keywords:
- amino-cyclodextrin;
- multiwalled carbon nanotubes;
- bovine serum albumin;
- secondary structure
Abstract
A novel amino-cyclodextrin was synthesized, and it was covalently attached to multiwalled carbon nanotubes (MWNTs). The functionalized MWNTs (f-MWNTs) have very good aqueous dispersibility. Bovine serum albumin (BSA) was adsorbed onto f-MWNTs through noncovalent interactions, including the hydrophobic interaction of the residues of BSA with the wall of MWNT and the guest–host interaction of the residues with the cyclodextrin (CD) moieties of f-MWNTs. The ultraviolet–visible (UV–vis) absorption of the f-MWNT-BSA hybrid was measured with UV–vis spectrometer, and the absorbance can be described well with the Beer–Lambert law. The X-ray diffraction patterns have indicated that the crystalline form of BSA has been changed after the adsorption of BSA on f-MWNTs. The circular dichroism spectra have shown that a high percentage of α-helical content can be retained for BSA adsorbed on f-MWNTs. The results also indicate that the change of secondary structure of BSA is mainly due to the hydrophobic interaction of the residues of BSA with the wall of f-MWNT, whereas the secondary structure is much less affected by the interaction of the CD moieties with BSA. © 2011 American Institute of Chemical Engineers AIChE J, 2011