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Scolopendin 2, a cationic antimicrobial peptide from centipede, and its membrane-active mechanism
- Source :
- Biochimica et Biophysica Acta (BBA) - Biomembranes. 1848(2):634-642
- Publication Year :
- 2015
- Publisher :
- Elsevier BV, 2015.
-
Abstract
- Scolopendin 2 is a 16-mer peptide (AGLQFPVGRIGRLLRK) derived from the centipede Scolopendra subspinipes mutilans. We observed that this peptide exhibited antimicrobial activity in a salt-dependent manner against various fungal and bacterial pathogens and showed no hemolytic effect in the range of 1.6μM to 100μM. Circular dichroism analysis showed that the peptide has an α-helical properties. Furthermore, we determined the mechanism(s) of action using flow cytometry and by investigating the release of intracellular potassium. The results showed that the peptide permeabilized the membranes of Escherichia coli O157 and Candida albicans, resulting in loss of intracellular potassium ions. Additionally, bis-(1,3-dibutylbarbituric acid) trimethine oxonol and 3,3′-dipropylthiacarbocyanine iodide assays showed that the peptide caused membrane depolarization. Using giant unilamellar vesicles encapsulating calcein and large unilamellar vesicles containing fluorescein isothiocyanate-dextran, which were similar in composition to typical E. coli O157 and C. albicans membranes, we demonstrated that scolopendin 2 disrupts membranes, resulting in a pore size between 4.8nm and 5.0nm. Thus, we have demonstrated that a cationic antimicrobial peptide, scolopendin 2, exerts its broad-spectrum antimicrobial effects by forming pores in the cell membrane.
- Subjects :
- Circular dichroism
Erythrocytes
Scolopendin 2
Amino Acid Motifs
Molecular Sequence Data
Biophysics
Peptide
Membrane damage
Microbial Sensitivity Tests
Escherichia coli O157
Biochemistry
Arthropod Proteins
Cell membrane
chemistry.chemical_compound
Anti-Infective Agents
Candida albicans
medicine
Animals
Humans
Benzothiazoles
Arthropods
Unilamellar Liposomes
Fluorescent Dyes
chemistry.chemical_classification
biology
Vesicle
Cell Membrane
Scolopendra subspinipes mutilans
Dextrans
Isoxazoles
Cell Biology
Carbocyanines
biology.organism_classification
Antimicrobial
Fluoresceins
Calcein
medicine.anatomical_structure
Membrane
Spectrometry, Fluorescence
chemistry
Barbiturates
Antimicrobial peptide
Fluorescein-5-isothiocyanate
Antimicrobial Cationic Peptides
Subjects
Details
- ISSN :
- 00052736
- Volume :
- 1848
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Accession number :
- edsair.doi.dedup.....183614eb3df7773c76dcda954622a2e5
- Full Text :
- https://doi.org/10.1016/j.bbamem.2014.11.016