Structure and Function of Enzymes Adsorbed onto Single-Walled Carbon Nanotubes
Top Cited Papers
- 16 November 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Langmuir
- Vol. 20 (26) , 11594-11599
- https://doi.org/10.1021/la047994h
Abstract
We have examined the structure and function of two enzymes, α-chymotrypsin (CT) and soybean peroxidase (SBP), adsorbed onto single-walled carbon nanotubes (SWNTs). SBP retained up to 30% of its native activity upon adsorption, while the adsorbed CT retained only 1% of its native activity. Analysis of the secondary structure of the proteins via FT-IR spectroscopy revealed that both enzymes undergo structural changes upon adsorption, with substantial secondary structural perturbation observed for CT. Consistent with these results, AFM images of the adsorbed enzymes indicated that SBP retains its native three-dimensional shape while CT appears to unfold on the SWNT surface. This study represents the first in depth investigation of protein structure and function on carbon nanotubes, which is critical in designing optimal carbon nanotube−protein conjugates.Keywords
This publication has 30 references indexed in Scilit:
- Nanotube Molecular Transporters: Internalization of Carbon Nanotube−Protein Conjugates into Mammalian CellsJournal of the American Chemical Society, 2004
- Protein-Affinity of Single-Walled Carbon Nanotubes in WaterThe Journal of Physical Chemistry B, 2004
- Effects of Potassium Bromide Disk Formation on the Infrared Spectra of Dried Model ProteinsJournal of Pharmaceutical Sciences, 2004
- Noncovalent Functionalization of Graphite and Carbon Nanotubes with Polymer Multilayers and Gold NanoparticlesNano Letters, 2003
- Protein Electrochemistry Using Aligned Carbon Nanotube ArraysJournal of the American Chemical Society, 2003
- Attaching Proteins to Carbon Nanotubes via Diimide-Activated AmidationNano Letters, 2002
- Functionalization of Carbon Nanotubes for Biocompatibility and Biomolecular RecognitionNano Letters, 2002
- Structure of soybean seed coat peroxidase: A plant peroxidase with unusual stability and haem‐apoprotein interactionsProtein Science, 2001
- Crystal and molecular structure of the bovine α-chymotrypsin-eglin c complex at 2.0 Å resolutionJournal of Molecular Biology, 1992
- Protein secondary structures in water from second-derivative amide I infrared spectraBiochemistry, 1990