Because of their extraordinary electronic and mechanical properties, carbon nanotubes have great potential as materials for applications ranging from molecular electronics to ultrasensitive biosensors. Biological molecules interacting with carbon nanotubes provide them with specific chemical handles that would make several of these applications possible. Here we use phage display to identify peptides with selective affinity for carbon nanotubes. Binding specificity has been confirmed by demonstrating direct attachment of nanotubes to phage and free peptides immobilized on microspheres. Consensus binding sequences show a motif rich in histidine and tryptophan, at specific locations. Our analysis of peptide conformations shows that the binding sequence is flexible and folds into a structure matching the geometry of carbon nanotubes. The hydrophobic structure of the peptide chains suggests that they act as symmetric detergents.