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Redox-regulated ion channel activity of a cysteine-containing gramicidin A analogue
- Source :
- Biochimica et Biophysica Acta (BBA) - Biomembranes. (4):493-498
- Publisher :
- Elsevier B.V.
-
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.
- Subjects :
- Transmembrane peptide
Biophysics
Peptide
Biochemistry
Redox
Ion Channels
chemistry.chemical_compound
Organic chemistry
Amino Acid Sequence
Cysteine
Ion channel
chemistry.chemical_classification
Liposome
Phospholipid membrane
Gramicidin
Cell Biology
Hydrogen Peroxide
Amino acid
Anti-Bacterial Agents
Kinetics
Membrane
chemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Oligopeptides
Oxidation-Reduction
Subjects
Details
- Language :
- English
- ISSN :
- 00052736
- Issue :
- 4
- Database :
- OpenAIRE
- Journal :
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Accession number :
- edsair.doi.dedup.....15d94d1400dc47b8633f19f9d44e25da
- Full Text :
- https://doi.org/10.1016/j.bbamem.2006.02.028