Probing Melittin Helix−Coil Equilibria in Solutions and Vesicles

Abstract

Melittin is a toxic, amphipathic peptide that rearranges from a random coil in solution to a helical structure upon binding to cell membranes or lipid vesicles. We have found that mutation of the valine at position five of the peptide to a phenylalanine or 3-nitrotyrosine induces aggregation and helix formation at low concentrations (20−80 μM). Donor−acceptor distances obtained from analyses of fluorescence energy transfer kinetics experiments with the 3-nitrotyrosine mutant indicate that both coil and helix structures are present in 2 and 20 μM aqueous solutions. The helical peptide population increases upon addition of phospholipid vesicles or in high ionic strength solutions.

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