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The rapid dissemination of antibiotic resistance accelerates the desire for new antibacterial agents. Here, a class of antimicrobial peptides (AMPs) is designed by modifying the structural parameters of a natural chickpea-derived AMP-Leg2, termed "functionalized chickpea-derived Leg2 antimicrobial peptides" (FCLAPs). Among the FCLAPs, KTA and KTR show superior antibacterial efficacy against the foodborne pathogen Escherichia coli (E. coli) O157:H7 (with MICs in the range of 2.5-4.7 μmol L −1 ) and demonstrate satisfactory feasibility in alleviating E. coli O157:H7-induced intestinal infection. Additionally, the low cytotoxicity along with insusceptibility to antimicrobial resistance increases the potential of FCLAPs as appealing antimicrobials. Combining the multi-omics profiling andpeptide-membrane interaction assays, a unique dual-targeting mode of action is characterized. To specify the antibacterial mechanism, microscopical observations, membrane-related physicochemical properties studies, and mass spectrometry assays are further performed. Data indicate that KTA and KTR induce membrane damage by initially targeting the lipopolysaccharide (LPS), thus promoting the peptides to traverse the outer membrane. Subsequently, the peptides intercalate into the peptidoglycan (PGN) layer, blocking its synthesis, and causing a collapse of membrane structure. These findings altogether imply the great potential of KTA and KTR as promising antibacterial candidates in combating the growing threat of E. coli O157:H7.

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Antibacterial materials are urgently needed to combat bacterial contamination, growth, or attachment on contact surfaces, as bacterial infections remain a public health crisis worldwide. Here, a novel ultrasound-assisted method is utilized for the first time to fabricate oxidative chlorine-loaded AH@PBAT/ PBF-Cl films with more superior grafting efficiency and rechargeable antibacterial effect than those from conventional techniques. The films remarkably inactivate 99.9999% Escherichia coli and Staphylococcus aureus cells, inducing noticeable cell deformations and mechanical instability. The specific antibacterial mechanism against E. coli used as a model organism is unveiled using several cell envelope structural and functional analyses combined with proteomics, peptidoglycomics, and fluorescence probe techniques. Film treatment partially neutralizes the bacterial surface charge, induces oxidative stress and cytoskeleton deformity, alters membrane properties, and disrupts the expression of key proteins involved in the synthesis and transport of the lipopolysaccharide and peptidoglycan, indicating the cell envelope as the primary target. The films specifically target lipopolysaccharides, resulting in structural impairment of the polysaccharide and lipid A components, and inhibit peptidoglycan precursor synthesis. Together, these lead to metabolic disorders, membrane dysfunction, structural collapse, and eventual death. Given the films' antibacterial effects via the disruption of key cell envelope components, they can potentially combat a wide range of bacteria. These findings lay a theoretical basis for developing efficient antibacterial materials for food safety or biomedical applications.