Mode of action and membrane specificity of the antimicrobial peptide snakin-2
Antimicrobial peptides (AMPs) are a diverse group of short, cationic peptides which are naturally occurring molecules in the first-line defense of most living organisms. They represent promising candidates for the treatment of pathogenic microorganisms. Snakin-2 (SN2) from tomato (Solanum lycopersic...
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| Format: | Article |
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PeerJ Inc.
2016-05-01
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| Series: | PeerJ |
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| Online Access: | https://peerj.com/articles/1987.pdf |
| _version_ | 1797417807975022592 |
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| author | Vera Herbel Michael Wink |
| author_facet | Vera Herbel Michael Wink |
| author_sort | Vera Herbel |
| collection | DOAJ |
| description | Antimicrobial peptides (AMPs) are a diverse group of short, cationic peptides which are naturally occurring molecules in the first-line defense of most living organisms. They represent promising candidates for the treatment of pathogenic microorganisms. Snakin-2 (SN2) from tomato (Solanum lycopersicum) is stabilized through six intramolecular disulphide bridges; it shows broad-spectrum antimicrobial activity against bacteria and fungi, and it agglomerates single cells prior to killing. In this study, we further characterized SN2 by providing time-kill curves and corresponding growth inhibition analysis of model organisms, such as E. coli or B. subtilis. SN2 was produced recombinantly in E. coli with thioredoxin as fusion protein, which was removed after affinity purification by proteolytic digestion. Furthermore, the target specificity of SN2 was investigated by means of hemolysis and hemagglutination assays; its effect on plant cell membranes of isolated protoplasts was investigated by microscopy. SN2 shows a non-specific pore-forming effect in all tested membranes. We suggest that SN2 could be useful as a preservative agent to protect food, pharmaceuticals, or cosmetics from decomposition by microbes. |
| first_indexed | 2024-03-09T06:24:02Z |
| format | Article |
| id | doaj.art-96d643a34f784464926fb5cbfe98ede8 |
| institution | Directory Open Access Journal |
| issn | 2167-8359 |
| language | English |
| last_indexed | 2024-03-09T06:24:02Z |
| publishDate | 2016-05-01 |
| publisher | PeerJ Inc. |
| record_format | Article |
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| spelling | doaj.art-96d643a34f784464926fb5cbfe98ede82023-12-03T11:29:43ZengPeerJ Inc.PeerJ2167-83592016-05-014e198710.7717/peerj.1987Mode of action and membrane specificity of the antimicrobial peptide snakin-2Vera Herbel0Michael Wink1Institute of Pharmacy and Molecular Biotechnology, Ruprecht-Karls-Universität Heidelberg, Heidelberg, GermanyInstitute of Pharmacy and Molecular Biotechnology, Ruprecht-Karls-Universität Heidelberg, Heidelberg, GermanyAntimicrobial peptides (AMPs) are a diverse group of short, cationic peptides which are naturally occurring molecules in the first-line defense of most living organisms. They represent promising candidates for the treatment of pathogenic microorganisms. Snakin-2 (SN2) from tomato (Solanum lycopersicum) is stabilized through six intramolecular disulphide bridges; it shows broad-spectrum antimicrobial activity against bacteria and fungi, and it agglomerates single cells prior to killing. In this study, we further characterized SN2 by providing time-kill curves and corresponding growth inhibition analysis of model organisms, such as E. coli or B. subtilis. SN2 was produced recombinantly in E. coli with thioredoxin as fusion protein, which was removed after affinity purification by proteolytic digestion. Furthermore, the target specificity of SN2 was investigated by means of hemolysis and hemagglutination assays; its effect on plant cell membranes of isolated protoplasts was investigated by microscopy. SN2 shows a non-specific pore-forming effect in all tested membranes. We suggest that SN2 could be useful as a preservative agent to protect food, pharmaceuticals, or cosmetics from decomposition by microbes.https://peerj.com/articles/1987.pdfSnakin-2Antimicrobial peptidePore-forming activityNon-specificBactericideFungicide |
| spellingShingle | Vera Herbel Michael Wink Mode of action and membrane specificity of the antimicrobial peptide snakin-2 PeerJ Snakin-2 Antimicrobial peptide Pore-forming activity Non-specific Bactericide Fungicide |
| title | Mode of action and membrane specificity of the antimicrobial peptide snakin-2 |
| title_full | Mode of action and membrane specificity of the antimicrobial peptide snakin-2 |
| title_fullStr | Mode of action and membrane specificity of the antimicrobial peptide snakin-2 |
| title_full_unstemmed | Mode of action and membrane specificity of the antimicrobial peptide snakin-2 |
| title_short | Mode of action and membrane specificity of the antimicrobial peptide snakin-2 |
| title_sort | mode of action and membrane specificity of the antimicrobial peptide snakin 2 |
| topic | Snakin-2 Antimicrobial peptide Pore-forming activity Non-specific Bactericide Fungicide |
| url | https://peerj.com/articles/1987.pdf |
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