Site-Specific Attachment of a Protein to a Carbon Nanotube End without Loss of Protein Function

http://pubs.acs.org/doi/full/10.1021/bc300131w

Bioconjugate Chemistry

The authors attached calmodulin to the ends of carbon nanotubes and demonstrated that the binding capacity of calmodulin remained unchanged. Protein attachment was done via a site-specific mutation of Tyr80 to azido-tyrosine, which was then coupled to oxidized CNTs using a Staudinger-Bertozzi ligation. Calmodulin binding was demonstrated using an ECFP-calmodulin-binding peptide fusion protein. Treatment with ECFP-CBP showed binding only on the ends of the CNTs.