“We’ve been using Edman sequencing to map the amino acid composition of our peptides, but these new approaches have the potential to transform the way we do venom research,” he says. “Each cone snail species has over a thousand unique peptides, not to mention a host of protein machinery that makes and modifies these peptides, and these new technologies are going to be essential in helping us uncover all variations that occur in this amazing group of molecules and give us clues to how they first evolved.”

JBC Highlight: Sharpe, I. A., Palant, E., Schroeder, C. I., Kaye, D. M., Adams, D. J., Alewood, P. F., and Lewis, R. J. (2003) Inhibition of the norepinephrine transporter by the venom peptide χ-MrIA: site of action, Na+ dependence and structure-activity relationship. J. Biol. Chem. 278, 40317 – 40323.

Nick Zagorski (nzagorski@asbmb.org) is a science writer at ASBMB.