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...

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Published in:PeerJ (San Francisco, CA) CA), 2015-12, Vol.3, p.e1516-e1516, Article e1516
Main Authors: Brannan, Alexander M, Whelan, William A, Cole, Emma, Booth, Valerie
Format: Article
Language:English
Subjects:
Antibiotics
Antimicrobial agents
Antimicrobial peptides
Bacteria
Biochemistry
Biology
Biophysics
Calorimetry
Differential scanning calorimetry
Differential Scanning Calorimetry (DSC)
E coli
Escherichia coli
Hydrophobicity
Infectious Diseases
Kanamycin
Lipids
Membrane active peptides
Membranes
NMR
Nuclear magnetic resonance
Pathogens
Peptides
Ratios
Ribosomes
Spectrum analysis
Studies
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Summary: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.
ISSN:2167-8359
2167-8359
DOI:10.7717/peerj.1516