Abstract:  Polypeptide toxins that block voltage-gated ion channels, usually with high potency and sub-type selectivity, are promising leads for the development of novel therapeutic agents. The design of some truncated and stabilised peptide analogues of ShK toxin and their conformational evaluation by NMR will be described. The structures of another polypeptide toxin determined recently will also be described briefly. In addition, solid-state NMR has been used to study the effect of EqT II on the structure and dynamics of membrane lipids in bilayers both in the presence and absence of sphingomyelin. Strategies for determining the structure of the active pore of this toxin (probably a tetramer) in a membrane bilayer will be discussed.

Resume:  Ray Norton received his B.Sc.(HONS) from the University of Melbourne and his PhD from ANU. He has won a number of distinguished awards and held various positions at Roche, ANU, UNSW, Univ. Washington, Oxford Univ., Univ. Melbourne and La Trobe. He has been a past president of the Aust. Society for Biophysics and has sat on NH&MRC panels. Dr. Norton has published over 140 papers in peer-reviewed journals, 8 book chapters and 12 invited reviews.