Redox-regulated ion channel activity of a cysteine-containing gramicidin A analogue

Biochimica Et Biophysica Acta
Yuri N AntonenkoAndrey Y Surovoy

Abstract

According to recent data, gramicidin A analogues having positively charged amino acid sequences at the C-termini exhibit two types of channel activity in lipid membranes: classical cation-selective channels and large unselective pores. The induction of unselective pores was shown here to strongly depend on the redox state of the membrane-bathing solution, if the gramicidin analogue contained a cysteine residue in the sequence GSGPKKKRKVC attached to the C-terminus. In particular, the addition of H2O2 led to an increase in the transmembrane current and the loss of cationic selectivity on planar bilayer lipid membranes and an increase in the carboxyfluorescein leakage of liposomes. The effect was observed at high concentration of the peptide while was absent at the single-channel level. It was concluded that oxidation led to possible formation of dimers of the peptide, which promoted the formation of large unselective pores.

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Citations

Nov 2, 2011·European Biophysics Journal : EBJ·Tatyana I RokitskayaYuri N Antonenko
Jun 29, 2013·Biochimica Et Biophysica Acta·Alexandra I SorochkinaYuri N Antonenko
Mar 15, 2008·Biochimica Et Biophysica Acta·Tatiana B StoilovaVadim T Ivanov

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