Exploring the Potential of MPC-A5K,A8K Analog Derived from Mastoparan C as an Alternative to Preservatives

Abstract

Antimicrobial peptides, renowned for their diverse biological properties, hold significant potential as sources for developing new pharmaceutical agents and food preservatives. A recent study investigating various derivatives of the natural peptide Mastoparan C revealed that the peptide MPC-A5K,A8K exhibited strong antimicrobial activity with low toxicity to human red blood cells. In this study, MPC-A5K,A8K’s antimicrobial effectiveness was compared to several antibiotics, and its preservative potential in oral formulations was preliminarily evaluated. The peptide MPC-A5K,A8K was synthesized through solid-phase peptide synthesis, with alanine residues at positions 5 and 8 in Mastoparan C replaced by lysine. The product achieved a purity of 98.1%, with an overall synthesis efficiency of 31.2%. This MPC-A5K,A8K derivative demonstrated broad-spectrum antimicrobial activity, including Gram-positive and Gram-negative bacteria as well as the fungus Candida albicans, with minimum inhibitory concentrations (MICs) ranging from 4 to 64 μM. In preliminary preservative efficacy tests, incorporating 10 ppm of MPC-A5K,A8K in formulations allowed for a reduction in sodium benzoate and potassium sorbate concentrations to 0.1% each while maintaining effective preservative properties. These promising findings lay a foundation for further research into the potential applications of MPC-A5K,A8K as a dual antimicrobial and preservative agents.