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Protein Science, Vol 7, Issue 12 2567-2577, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Interaction of wheat {alpha}-thionin with large unilamellar vesicles

JMM. CAAVEIRO, A. MOLINA, P. RODRIGUEZ-PALENZUELA, F. M. GONI and J. M. GONZALEZ-MANAS
Grupo Biomembranas (Unidad Asociada al CSIC), Departamento de Bioquimica y Biologia Molecular, Universidad del Pais Vasco, Apdo. 644, 48080 Bilbao, Spain

The interaction of the wheat antibacterial peptide {alpha}-thionin with large unilamellar vesicles has been investigated by means of fluorescence spectroscopy. Binding of the peptide to the vesicles is followed by the release of vesicle contents, vesicle aggregation, and lipid mixing. Vesicle fusion, i.e., mixing of the aqueous contents, was not observed. Peptide binding is governed by electrostatic interactions and shows no cooperativity. The amphipatic nature of wheat {alpha}-thionin seems to destabilize the membrane bilayer and trigger the aggregation of the vesicles and lipid mixing. The presence of distearoylphosphatidylethanolamine-poly(ethylene glycol 2000) (PEG-PE) within the membrane provides a steric barrier that inhibits vesicle aggregation and lipid mixing but does not prevent leakage. Vesicle leakage through discrete membrane channels is unlikely, because the release of encapsulated large fluorescent dextrans is very similar to that of 8-aminonaphthalene-1,3,6,trisulfonic acid (ANTS). A minimum number of 700 peptide molecules must bind to each vesicle to produce complete leakage, which suggests a mechanism in which the overall destabilization of the membrane is due to the formation of transient pores rather than discrete channels.
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