The antimicrobial peptide (AMP) comprising a repeating (RW)n unit (n=6) and amidation at C-terminus has been shown to have a high destructive effect on bacterial model membranes. A proline residue was introduced in the middle of the AMP. Proline is often used as inducer of distinct conformations or breaking helices. The effect of proline incorporation on the structure, morphology and activity of the AMP was investigated using infrared (IR), scanning electron microscopy (SEM), thermogravimetric analysis (TGA) and differential scanning calorimetry (DSC). Zwitterionic dipalmitoylphosphocholine (DPPC) and anionic palmitoyloleoylphosphoglycerol (POPG) lipids were chosen as models for, respectively, eukaryotic and bacterial membranes. Infrared curve fitting results indicate that proline increased the beta-sheet structure content in the AMP by breaking the helix structures. TGA and DSC data show a lipid clustering effect due to proline. SEM revealed a stronger interaction of the proline containing AMP with DPPC than that of the proline-free one. The preference for DPPC suggests that the proline containing AMP would be very effective against Gram-negative pathogens that are resistant to many antibiotics due to their drug-impermeable cell wall

Effect of incorporating a proline residue into an antimicrobial peptide comprising a repeating (RW)n unit on the structure, morphology and selectivity

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