Abstract
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
Highlights
antimicrobial peptide (AMP) are a crucial component of the innate immune system of many organisms and can protect against a variety of invading pathogens including bacteria, viruses, and microbial eukaryotes (Shai, 1999; Zasloff, 2002; Jenssen, Hamill & Hancock, 2006; Nguyen, Haney & Vogel, 2011; Wimley & Hristova, 2011; Bechinger & Salnikov, 2012)
We describe differential scanning calorimetry (DSC) studies of the AMP MSI-78 interacting with whole bacteria
Differential scanning calorimetry was used to assess the thermal transitions in whole E. coli JM109 cells upon addition of increasing concentrations of MSI-78 and small molecule antibiotics
Summary
AMPs are a crucial component of the innate immune system of many organisms and can protect against a variety of invading pathogens including bacteria, viruses, and microbial eukaryotes (Shai, 1999; Zasloff, 2002; Jenssen, Hamill & Hancock, 2006; Nguyen, Haney & Vogel, 2011; Wimley & Hristova, 2011; Bechinger & Salnikov, 2012). AMPs have been isolated from a plethora of organisms, including plants, humans, frogs, and bacterial species. They are generally short, typically ranging from 12 to 50 amino acids in length, cationic, due to an abundance of basic residues (lysine, arginine, histidine), and amphipathic, with some AMPs displaying a hydrophobicity of >50%. By focusing solely on the lipids, studies that are limited to model membrane systems fail to capture the myriad of potentially important interactions that AMPs may have with their target microbes
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