Structure and Function of Enzymes Adsorbed onto Single-Walled Carbon Nanotubes

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 o...

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Bibliographic Details
Published in:Langmuir 2004-12, Vol.20 (26), p.11594-11599
Main Authors: Karajanagi, Sandeep S, Vertegel, Alexey A, Kane, Ravi S, Dordick, Jonathan S
Format: Article
Language:English
Subjects:
Animals
Binding Sites
Cattle
Chymotrypsin - chemistry
Chymotrypsin - metabolism
Enzymes, Immobilized - chemistry
Enzymes, Immobilized - metabolism
Glycine max - enzymology
Hydrophobic and Hydrophilic Interactions
Microscopy, Atomic Force
Models, Molecular
Nanotubes, Carbon - chemistry
Nanotubes, Carbon - ultrastructure
Peroxidase - chemistry
Peroxidase - metabolism
Protein Structure, Secondary
Protein Structure, Tertiary
Spectroscopy, Fourier Transform Infrared
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Summary: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.
ISSN:0743-7463
1520-5827
DOI:10.1021/la047994h