Publication:
PAPAIN-CATALYZED SYNTHESIS OF ALTERNATING ARGININE-TRYPTOPHAN PEPTIDES FOR ANTIMICRIOBIAL APPLICATIONS

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2026-04-16
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Antimicrobial peptides represent a promising strategy for combating multidrug resistant pathogens. However, the conventional synthesis strategy using Solid Phase Peptide Synthesis (SPPS) relies on harsh reagents, extensive solvent use and costly, multi-step protocols. In this study, we investigate a greener and more efficient approach to synthesizing peptides using Protease-Catalyzed Peptide Synthesis (PCPS) to generate short arginine-tryptophan (Arg-Trp) peptides, molecules known to possess antimicrobial properties. We examine the enzymatic coupling of Arg-Trp dipeptides using papain, a well-documented protease, as a biocatalyst under mild conditions, promoting peptide bond formation through aminolysis rather than hydrolysis. The reaction products are characterized by MALDI-TOF mass spectrometry to assess peptide formation and composition. This approach aims to provide a cost-effective and environmentally sustainable alternative to traditional peptide synthesis, with findings that will inform future studies on alternative syntheses and antimicrobial efficacy of Arg–Trp peptides produced via PCPS.
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