Antimicrobial peptides (AMPs) are considered a potential candidate to develop a newer generation of antibiotics against multi-drug-resistant pathogenic bacteria. We recently developed potent cyclic AMPs named [H2R2W4] containing histidine, arginine, and tryptophan amino acid. The stability and toxicity of AMPs are a major hurdle for clinical application. Therefore, we hypothesized to use the N-methylation strategy in the peptide backbone to modulate stability and cytotoxicity against mammalian cells. A series of N-methylated H2R2W4 peptides were designed and synthesized using Fmoc/tBu solid-phase peptide synthesis. Peptides were characterized using matrix-assisted laser desorption/ionization mass spectrometry and purified using reverse-phase high-performance liquid chromatography. Synthesized peptides will be evaluated for antibacterial activity against Gram-positive and Gram-negative pathogenic bacteria. The biophysical characterization using circular dichroism, cytotoxicity, and stability will be reported.

Design, synthesis, and evaluation of antibacterial activity of N-methylated H2R2W4 peptides

ACS Spring 2022

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