Scientists created a simple way to make a synthetic peptide mixture that looks like the natural antimicrobial peptide LL‑37. The mixture (called KLS‑3) kills a range of harmful bacteria, including tough strains like MRSA, at low microgram concentrations in lab tests. However, the study only shows lab‑based antibacterial activity and doesn’t give guidance on how to use it in people.

A facile method has been developed for the large-scale synthesis of random copolypeptides composed of multiple (i.e., cationic, hydrophobic, and hydrophilic) amino acids and their relative ratios have been optimized for broad-spectrum antibacterial effect. The copolypeptides obtained have measured compositions close to the design ratios in spite of the differing reactivities of the different amino acids. An optimized random copolypeptide of lysine, leucine, and serine (denoted as KLS-3) mimicking the composition of LL-37 host defense peptide gives broad spectrum antibacterial activity against clinically relevant Gram-negative and Gram-positive bacteria such as methicillin-resistant Staphylococcus aureus (MRSA) and Pseudomonas aeruginosa (PAO1) with minimum inhibitory concentrations (MICs) of 32-64 μg mL^-1 , as well as good MICs against multidrug resistant Gram-negative bacteria of Escherichia coli EC 958 (64 μg mL^-1 ) and Klebseilla pneumoniae PTR3 (128 μg mL^-1 ). This method can be applied to the facile large-scale copolymerization of multiple amino acids, including unnatural amino acids, to make effective antibacterial copolypeptides.