Using the M13 phage display method, 236 amino acid sequences
(peptide
aptamers) that could specifically adsorb to CNTs were selected. These
peptide aptamers had abundant hydrophobic amino acids and evenly dispersed
charged amino acids. The hydrophobic amino acids were postulated to
contribute to CNT adsorption, while the charged amino acids contribute
to their aqueous solubility. The frequency of proline amino acids,
which causes the amino acid main chain bending, was slightly higher
than in nature, suggesting that some conformational constraint might
be required. Four peptide aptamers with a high frequency of occurrence
in the selected sequences were further studied. Hydrophobicity scores
were periodic along the amino acid sequence. 3D structure predictions
by PEP-FOLD3 indicated that these aptamers would take a helical structure
with hydrophobic amino acid residues on one side, suggesting that
the aptamers bind hydrophobically to the CNT. The adsorption of these
four aptamers to the carbon electrode was confirmed by electrochemical
impedance spectroscopy, which demonstrated the effectiveness of the
phage display method. At the same time, it was shown that even for
selected peptides, the adsorption performance varied, and verification
was needed.