Peptides have shown great potential as components of novel materials, as therapeutics and as therapeutic carriers. While small peptides can be made efficiently through chemical synthesis, larger peptides (&gt;30 residues) can be difficult to synthesize and are too sensitive to protease degradation to be made using traditional recombinant methods. Bacillus megaterium is a Gram-positive host that couples efficient secretion with low extracellular protease activity, making it an intriguing host for recombinant peptide production. Secretion from recombinant hosts requires the additional of a small signal peptide (SP) to the N-terminus of the target protein, and has been an underutilized tool for engineers because of a relatively unclear compatibility requirement between the two. We will describe the design and characterization of a novel, modular system for efficient peptide secretion from B. megaterium. A key aspect of our system is consistent sequence and structure near the SP cleavage site. We hypothesize that this will lead to efficient secretion regardless of the target peptide. While our initial focus is on peptide production, we believe that this system will be an effective tool for secreting proteins of any size.

New method for peptide production: Modular secretion from Bacillus megaterium

249th National Meeting (2015)

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