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Antimicrobial peptides  (AMPs) were investigated both as novel antibiotics and as antimicrobial coatings for biomedical implants. The hydrophobicity, conformational constraint, and strong binding of cyclo‐RRRWFW (c‐WFW) to the  O ‐antigen region of lipopolysaccharide (LPS) were identified as important features for potent anti‐ E. coli  activity. Furthermore, tethered membrane‐active AMPs with uniform distribution of cationic and hydrophobic amino acid residue were identified as good anti‐biofilm agents.

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Cationic Antimicrobial Peptides (AMPs): Thermodynamic Characterization of Peptide–Lipid Interactions and Biological Efficacy of Surface‐Tethered Peptides