Intrinsic Charge-Shielding Effects of Bacteria Promote Rapid On-Surface Assembly of Random-Coil Oligopeptides for Enhanced Antibacterial Activity

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Bacteria-induced assembly of cationic oligopeptides via a charge shielding mechanism represents a promising strategy for improving the antibacterial capacity of oligopeptides. However, the impact of amino acid residues, sequence encoding, and charges on antibacterial activity remains to be more clearly elucidated. We designed random-coil oligopeptides ((RF)nR and (KF)nK (n = 2, 3, 4)) with alternating basic and phenylalanine residues to clarify their on-surface assembly and antibacterial performance. Keeping enough hydrophobic residues, the higher charges of the peptides or the potentials of bacteria, the stronger electrostatic affinity. Molecular dynamics simulations supported the stronger membrane association and near-interface clustering of the nonapeptides. As a result, random-coil (RF)4R and (KF)4K exhibited extremely rapid on-surface assembly and antibacterial kinetics against both Gram-negative (MIC ≤ 25 μM) and Gram-positive (MIC ≤ 50 μM) bacteria. This study establishes a primary principle for designing bacteria-responsive antibacterial oligopeptides.

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