Abstract:
Dispersion of single walled carbon nanotube in water is hard to achieve due to the strong cohesive forces existing between them. A good dispersion of nanotubes is essential for their separation into their chirality based separation. Many surfactants like SDS have been used to create a dispersion of nanotubes and for their separation into different chiralities (zig-zag, armchair and chiral). The dual action of these surfactants is assumed to be due to their amphiphilic nature of a hydrophobic core surrounded by a hydrophilic head. The interaction of carbon nanotubes with biological molecules has been less studied hence finding peptides which can disperse the bundle or ropes of nanotube while displaying selective affinity for different kinds of nanotube can expand the small list of surfactants existing today. In this study, we create a tripepetide library from the D3 domain of flagellin (used in previous study by Macwan et al.) All the 9 tri-peptides in the library showed the presence of a middle glycine residue. Their interactions with single walled carbon nanotubes was studied using Visual Molecular Dynamics (VMD). RMSD provided quantitative and qualitative data to determine the extent and selectivity of the interactions, hence allowing us to screen the tri-peptide library to determine the tri-peptides with the best selective affinity for the nanotubes.
