Pln149 peptide

Pln149a is a C-terminal amidated form of the peptide. Pln149a was active against one strain of S. aureus and four strains of Listeria genus at pH 5.5 and 7.4 and, like its natural variant, inhibited L. plantarum ATCC 8014. It is helical in TFE and a reverse micelle (Muller DM et al., 2007). The amidated form also inhibited the growth of fungi such as S. cerevisiae. Pln149a does not interact with either mono/polysaccharides or zwitterionic LUVs, but is strongly adsorbed to and incorporated into negatively charged surfaces, causing a conformational change in its secondary structure from random-coil to helix upon adsorption (Lopes JL et al., 2009). Fatty acid conjugation of shorter peptides with low antimicrobial activity resulted in lipopeptides with improved activity against strains of S. aureus and L. monocytogenes. The length of the fatty acid determined the bacterial specificity, and the conjugation with n-octanoic acid yielded the most active analog (C8-CT) against S. aureus (MIC: 1.0 uM) while the conjugation with n-dodecanoic acid (C12-CT) was optimal for L. monocytogenes (MIC: 2.0 uM)(Siano A et al., 2011). Updated 5/2014. Pln149 has Antibacterial activity. The source of Pln149 is Lactobacillus plantarum NRIC 149; isolated from pineapple.