Brannan, Alexander M. and Whelan, William A. and Cole, Emma and Booth, Valerie (2015) 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, 3. ISSN 2167-8359
- Published Version
Available under License Creative Commons Attribution Non-commercial.
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.
|Additional Information:||Memorial University Open Access Author's Fund|
|Keywords:||Antimicrobial peptides, Differential Scanning Calorimetry (DSC), Membrane active peptides|
|Department(s):||Science, Faculty of > Biochemistry
Science, Faculty of > Physics and Physical Oceanography
|Date:||17 December 2015|
|Library of Congress Subject Heading:||Biophysics, Infectious Diseases|
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