Peptide based molecular recognition elements for binding 2,4,6-trinitrotoluene

Three peptides labeled AS2, AS3 and AS6 were designed to evaluate the role of secondary structure in a peptide\u27s ability to selectively bind 2,4,6 trinitrotoluene (TNT). The peptides were produced using recombinant DNA methods through E. coli expression. It was hypothesized that AS6 would form a random coil, AS2 would form an alpha-helix and AS3 would form a beta-sheet. The secondary structures of the peptides were determined using circular dichroism spectroscopy and the binding of the peptides to TNT was studied using an enzyme linked immunosorbent assay. After expression, the presence of the peptide in the final purified product was tested using a variety of methods including amino acid analysis western blot, and mass spectrometry. It was concluded that the E. coli did not consistently produce the desired peptides or produced them at very low levels, which precluded conclusive assessment of the contribution of peptide secondary structure in binding TNT