Fluorescence studies of the interaction of trichorzianine A IIIc with model membranes.

The biological activity and the chemical structure of the lipophilic peptides, trichorzianines, suggested that these substances could act on membrane permeability. The interaction of a major component of trichorzianines, trichorzianine A IIIc (TA IIIc), a 19-residue peptaibol containing tryptophanol as C-terminal amino-alcohol, with some synthetic phospholipid vesicles (egg phosphatidylcholine (egg PC), dipalmitoylphosphatidylcholine (DPPC) and sterol-containing egg PC) was studied by fluorescence spectroscopy. TA IIIc was found to bind to lipid vesicles either in liquid-crystalline or gel state. The accessibility to the aqueous phase of the embedded peptide was examined for various phospholipid compositions by fluorescence quenching experiments. We found that incorporation of TA IIIc in egg PC vesicles leads to reduced accessibility of the C-terminal tryptophanol to external quenchers, whereas when sterols are present in the bilayer, this accessibility is higher, consistent with a higher exposure of the chromophore to the aqueous phase. TA IIIc was shown to induce leakage of vesicular entrapped material. Incorporation of sterols in the bilayer seems to influence the position of the bound peptide within the bilayer but not its action on the membrane permeability.