Natural and artificial antimicrobial peptide designs: A comparative study of Mastoparan C and BP52

Abstract Antimicrobial peptides (AMPs) are small, naturally occurring molecules that play a vital role in the innate immune systems of various organisms, ranging from bacteria to humans. Additionally, artificial AMPs are also designed and synthesized based on the common structure-activity relationships (SARs) found in natural ones. As part of our ongoing effort to explore the advantages and disadvantages of each source, this study focused on two representative helical AMPs: Mastoparan C (MPC) and BP52. While the former is derived from the venom of the European wasp Vespa crabro, the latter belongs to a group of artificially designed AMPs inspired by the structure of two natural peptides, Cecropin A and Melittin M. Our preliminary data suggests that BP52 exhibits similar antimicrobial activity to MPC but demonstrates significantly higher potency against the A427 cancer cell line. Taken together with the shorter length and reduced toxicity to human red blood cells, BP52 exhibited greater potential in drug development compared to its counterpart, MPC.