Conformation analysis of nucleic acids and proteins adsorbed on single-shell carbon nanotubes

This paper presents a concise review of the experimental and calculated data reported in the literature on the noncovalent interactions of DNA and proteins with the nonfunctionalized carbon nanotubes. Our Raman scattering and electron microscopy data on carbon nanotubes and SEIRA spectral data on changes in the conformational state of the main biological polymers (DNA, Poly, BSA, and RNase) in reactions with single-shell carbon nanotubes allowed us to define the character of noncovalent interactions in the tube biomolecule system. An analysis of the data showed that reactions of DNA with nanotubes lead to the binding on the surface of the nanotube and form stable complexes with van der Waals interactions, in which stacking plays the major role and which changes the hydrogen bonds in the biological molecule with structure rearrangements. Albumin and RNase are presumably adsorbed at the conventional binding sites of these proteins on the nanotube with participation of hydrophobic interaction and pi stacking, as indicated by structure rearrangements in proteins.