Differential scanning calorimetry of whole Escherichia coli treated with the antimicrobial peptide MSI-78 indicate a multi-hit mechanism with ribosomes as a novel target
Differential Scanning Calorimetry (DSC) of intact Escherichia coli (E. coli) was used to identify non-lipidic targets of the antimicrobial peptide (AMP) MSI-78. The DSC thermograms revealed that, in addition to its known lytic properties, MSI-78 also has a striking effect on ribosomes. MSI-78’s effe...
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doaj-402b13d8f3ba405eb3bc2854eb2d7a442020-11-24T22:29:41ZengPeerJ Inc.PeerJ2167-83592015-12-013e151610.7717/peerj.1516Differential scanning calorimetry of whole Escherichia coli treated with the antimicrobial peptide MSI-78 indicate a multi-hit mechanism with ribosomes as a novel targetAlexander M. Brannan0William A. Whelan1Emma Cole2Valerie Booth3Department of Biochemistry, Memorial University of Newfoundland, St. John’s Newfoundland and Labrador, CanadaDepartment of Biochemistry, Memorial University of Newfoundland, St. John’s Newfoundland and Labrador, CanadaDepartment of Biochemistry, Memorial University of Newfoundland, St. John’s Newfoundland and Labrador, CanadaDepartment of Biochemistry, Memorial University of Newfoundland, St. John’s Newfoundland and Labrador, CanadaDifferential Scanning Calorimetry (DSC) of intact Escherichia coli (E. coli) was used to identify non-lipidic targets of the antimicrobial peptide (AMP) MSI-78. The DSC thermograms revealed that, in addition to its known lytic properties, MSI-78 also has a striking effect on ribosomes. MSI-78’s effect on DSC scans of bacteria was similar to that of kanamycin, an antibiotic drug known to target the 30S small ribosomal subunit. An in vitro transcription/translation assay helped confirm MSI-78’s targeting of ribosomes. The scrambled version of MSI-78 also affected the ribosome peak of the DSC scans, but required greater amounts of peptide to cause a similar effect to the unscrambled peptide. Furthermore, the effect of the scrambled peptide was not specific to the ribosomes; other regions of the DSC thermogram were also affected. These results suggest that MSI-78’s effects on E. coli are at least somewhat dependent on its particular structural features, rather than a sole function of its overall charge and hydrophobicity. When considered along with earlier work detailing MSI-78’s membrane lytic properties, it appears that MSI-78 operates via a multi-hit mechanism with multiple targets.https://peerj.com/articles/1516.pdfAntimicrobial peptidesDifferential Scanning Calorimetry (DSC)Membrane active peptides |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Alexander M. Brannan William A. Whelan Emma Cole Valerie Booth |
spellingShingle |
Alexander M. Brannan William A. Whelan Emma Cole Valerie Booth Differential scanning calorimetry of whole Escherichia coli treated with the antimicrobial peptide MSI-78 indicate a multi-hit mechanism with ribosomes as a novel target PeerJ Antimicrobial peptides Differential Scanning Calorimetry (DSC) Membrane active peptides |
author_facet |
Alexander M. Brannan William A. Whelan Emma Cole Valerie Booth |
author_sort |
Alexander M. Brannan |
title |
Differential scanning calorimetry of whole Escherichia coli treated with the antimicrobial peptide MSI-78 indicate a multi-hit mechanism with ribosomes as a novel target |
title_short |
Differential scanning calorimetry of whole Escherichia coli treated with the antimicrobial peptide MSI-78 indicate a multi-hit mechanism with ribosomes as a novel target |
title_full |
Differential scanning calorimetry of whole Escherichia coli treated with the antimicrobial peptide MSI-78 indicate a multi-hit mechanism with ribosomes as a novel target |
title_fullStr |
Differential scanning calorimetry of whole Escherichia coli treated with the antimicrobial peptide MSI-78 indicate a multi-hit mechanism with ribosomes as a novel target |
title_full_unstemmed |
Differential scanning calorimetry of whole Escherichia coli treated with the antimicrobial peptide MSI-78 indicate a multi-hit mechanism with ribosomes as a novel target |
title_sort |
differential scanning calorimetry of whole escherichia coli treated with the antimicrobial peptide msi-78 indicate a multi-hit mechanism with ribosomes as a novel target |
publisher |
PeerJ Inc. |
series |
PeerJ |
issn |
2167-8359 |
publishDate |
2015-12-01 |
description |
Differential Scanning Calorimetry (DSC) of intact Escherichia coli (E. coli) was used to identify non-lipidic targets of the antimicrobial peptide (AMP) MSI-78. The DSC thermograms revealed that, in addition to its known lytic properties, MSI-78 also has a striking effect on ribosomes. MSI-78’s effect on DSC scans of bacteria was similar to that of kanamycin, an antibiotic drug known to target the 30S small ribosomal subunit. An in vitro transcription/translation assay helped confirm MSI-78’s targeting of ribosomes. The scrambled version of MSI-78 also affected the ribosome peak of the DSC scans, but required greater amounts of peptide to cause a similar effect to the unscrambled peptide. Furthermore, the effect of the scrambled peptide was not specific to the ribosomes; other regions of the DSC thermogram were also affected. These results suggest that MSI-78’s effects on E. coli are at least somewhat dependent on its particular structural features, rather than a sole function of its overall charge and hydrophobicity. When considered along with earlier work detailing MSI-78’s membrane lytic properties, it appears that MSI-78 operates via a multi-hit mechanism with multiple targets. |
topic |
Antimicrobial peptides Differential Scanning Calorimetry (DSC) Membrane active peptides |
url |
https://peerj.com/articles/1516.pdf |
work_keys_str_mv |
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