T. Terry, P. Malek, R. N. Perham
Department of Biochemistry, University of Cambridge, Cambridge, England
Short amino acid sequences play major roles in molecular recognition and generation of immune response. Structure elucidation of short peptide [5-20 residues], however, has been limited by the absence of well- defined and stable conformations in solution, and fast molecular tumbling. We have explored several chemical and biological approaches to determine structures of short immunogenic peptides in environments which induce folding. We have carried out solution and solid state NMR experiments to determine the structures of immunogenic regions of HIV-1, and the foot-and-mouth disease virus, expressed on the major coat protein of filamentous phage. Evidence for peptide conformation was also obtained for short peptides displayed on polymer beads and liposomes. The NMR experiments suggest that conformations of short immunogenic sequences can be induced in solution through bonding of the peptides to larger chemical and biological entities.