iTRAQ-Based Quantitative Proteomic Analysis of the Antimicrobial Mechanism of Peptide F1 against Escherichia coli

Antimicrobial peptides have received
increasing attention in the
agricultural and food industries due to their potential to control
pathogens. However, to facilitate the development of novel peptide-based
antimicrobial agents, details regarding the molecular mechanisms of
these peptides need to be elucidated. The aim of this study was to
investigate the antimicrobial mechanism of peptide F1, a bacteriocin
found in Tibetan kefir, against Escherichia coli at protein levels using iTRAQ-based quantitative proteomic analysis.
In response to treatment with peptide F1, 31 of the 280 identified
proteins in E. coli showed alterations in their expression,
including 10 down-regulated proteins and 21 up-regulated proteins.
These 31 proteins all possess different molecular functions and are
involved in different molecular pathways, as is evident in referencing
the Kyoto Encyclopedia of Genes and Genomes pathways.
Specifically, pathways that were significantly altered in E. coli in response to peptide F1 treatment include the
tricarboxylic acid cycle, oxidative phosphorylation, glycerophospholipid
metabolism, and the cell cycle–caulobacter pathways, which
was also associated with inhibition of the cell growth, induction
of morphological changes, and cell death. The results provide novel
insights into the molecular mechanisms of antimicrobial peptides.