Antimicrobial peptides (AMPs) are a class of naturally occurring biomolecules found in all multicellular organisms and are used as a first line of defense for plants and animals against bacterial infection. At the molecular level, these peptides work either by rupturing the membrane or inhibiting intracellular function, resulting in bacterial lysis. The properties of AMPs allow for them to selectively bind to negatively charged membranes via electrostatic interactions, and selectively inhibit the growth of gram-positive and gram-negative bacteria, as well as certain fungi, and viruses. Low-molecular weight AMPs produced by bacteria, known as bacteriocins, have exceptional potency, narrow and broad killing spectrums, good pH stability, and low toxicity. Bacteriocins are classified into various groups based on their structure and functional characteristics. Laterosporulin is a novel defensin like class IId – linear one-peptide non-cyclic – bacteriocin from Brevibacillus sp. strain GI-9 with inhibitory activity against microbial pathogens. To investigate the structure-function relationships in the 50-amino acid AMP, recombinant laterosporulin was expressed in <i>E. coli</i> using the Champion pET SUMO protein expression system (ThermoFisher). Future work will involve the expression of various mutated peptides to probe the role of specific residues on the effectiveness of laterosporulin against gram-positive and gram-negative bacteria.

Expression of recombinant SUMO-tagged laterosporulin

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