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The rapid spread of multi\u2010drug\u2010resistant (MDR) bacteria is a global health emergency and there is a lack of new drugs to control MDR pathogens. We describe a heretofore\u2010unexplored discovery pathway for novel antibiotics that is based on self\u2010targeting, structure\u2010disrupting peptides. We show that a helical peptide, KFF\u2010\n                    <jats:italic>Ec<\/jats:italic>\n                    H3, derived from the\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    methionine aminopeptidase can disrupt secondary and tertiary structure of this essential enzyme, thereby killing the bacterium (including MDR strains). Significantly, no detectable resistance developed against this peptide. Based on a computational analysis, our study predicted that peptide KFF\u2010\n                    <jats:italic>Ec<\/jats:italic>\n                    H3 has the strongest interaction with the structural core of the methionine aminopeptidase. We further used our approach to identify peptide KFF\u2010\n                    <jats:italic>Ng<\/jats:italic>\n                    H1 to target the same enzyme from\n                    <jats:italic>Neisseria gonorrhoeae<\/jats:italic>\n                    . This peptide inhibited bacterial growth and was able to treat a gonococcal infection in a human cervical epithelial cell model. These findings present an exciting new paradigm in antibiotic discovery using self\u2010derived peptides that can be developed to target the structures of any essential bacterial proteins.\u2014Zhan, J., Jia, H., Semchenko, E. A., Bian, Y., Zhou, A. M., Li, Z., Yang, Y., Wang, J., Sarkar, S., Totsika, M., Blanchard, H., Jen, F. E.\u2010C., Ye, Q., Haselhorst, T., Jennings, M. P., Scib, K. L., Zhou, Y. Self\u2010derived structure\u2010disrupting peptides targeting methionine aminopeptidase in pathogenic bacteria: a new strategy to generate antimicrobial peptides. 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