Aggregation and ion transfer induced by tentoxin.
It is shown that tentoxin, a cyclic tetrapeptide with two N-methylated residues, is able, when added to lipid bilayers, to increase the transmembrane current through discrete events. Conformational investigations involving 1H-NMR, infrared and circular dichroism studies show that, at concentrations above 7 X 10(-5) M, the cyclic tetrapeptide aggregates in chloroform. We suggest that the aggregates could form a pore through a stacking of cycles.
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F
Heitz
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Jacquier
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Kaddari
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Verducci
D002942:Circular Dichroism; D004058:Diffusion; D006859:Hydrogen; D008051:Lipid Bilayers; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D008954:Models, Biological; D008958:Models, Molecular; D009183:Mycotoxins; D010456:Peptides, Cyclic; D010713:Phosphatidylcholines; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared
D008051:Lipid Bilayers; D046911:Macromolecular Substances; D009183:Mycotoxins; D010456:Peptides, Cyclic; D010713:Phosphatidylcholines; D006859:Hydrogen; C003384:tentoxin