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Aggregation and ion transfer induced by tentoxin.

F Heitz, R Jacquier, F Kaddari

Biophysical Chemistry

|March 1, 1986

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Tentoxin, a cyclic tetrapeptide, increases transmembrane current in lipid bilayers by forming pores. These pores result from the stacking of tentoxin aggregates observed at higher concentrations.

Area of Science:

Biophysics
Molecular Biology
Membrane Transport

Background:

Tentoxin is a cyclic tetrapeptide known for its biological activity.
Understanding the interaction of peptides with lipid bilayers is crucial for membrane transport studies.

Purpose of the Study:

To investigate the effect of tentoxin on transmembrane current in lipid bilayers.
To elucidate the mechanism by which tentoxin influences membrane permeability.

Main Methods:

Incorporation of tentoxin into artificial lipid bilayers.
Measurement of transmembrane electrical current.
Conformational analysis using 1H-NMR, infrared, and circular dichroism spectroscopy.
Investigation of tentoxin aggregation in chloroform.

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Main Results:

Tentoxin addition to lipid bilayers induced discrete events of increased transmembrane current.
Conformational studies revealed tentoxin aggregation in chloroform at concentrations above 7 X 10(-5) M.
Evidence suggests that stacked tentoxin aggregates may form transmembrane pores.

Conclusions:

Tentoxin can alter the permeability of lipid bilayers.
The observed increase in transmembrane current is likely mediated by tentoxin-formed pores.
Tentoxin aggregation plays a key role in pore formation and membrane interaction.