Controlling the covalent bonding of antibodies onto functionalized carbon nanotubes
is a key step in the design and preparation of nanotube-based conjugates for targeting
cancer cells. For this purpose, an anti-MUC1 antibody (Ab) is linked to both multiwalled
(MWCNTs) and double-walled carbon nanotubes (DWCNTs) using different
synthetic strategies. The presence of the Ab attached to the nanotubes is confi rmed
by gel electrophoresis and thermogravimetric analysis. Most importantly, molecular
recognition of the antigen by surface plasmon resonance is able to determine similar
Ab binding capacities for both Ab–DWCNTs and Ab–MWCNTs. These results are
very relevant for the design of future receptor-targeting strategies using chemically
functionalized carbon nanotubes.
