Mucroporin-M1 analogues: synthesis, conformation and structure-activity correlation

RESULTS CONCLUSIONSMucroporin is a peptide of 17 amino acids deriving from the scorpion venom Lychas mucronatus with known antimicrobial properties (active against gram-positive bacteria).Li et al. [1] optimized the Mucroporin sequence by proposing Mucroporin-M1 sequence with some amino acid substitutions (G3R, P6K, G10K and G11R).These modifications improved peptide activity at lower concentrations respect to the native peptide.Substitutions increase the net positive charge of the peptide, strengthening the amphipathic character of the peptide helix.Previous studies have shown that Mucroporin-M1 also possesses antiviral activity: it interacts directly with viral particles and that, when the peptide attaches to the virus, its strong electrostatic affinity increases the interaction and destruction of the viral envelope [1][2][3].The aim of this work was to further improve the activity of Mucroporin-M1 and develop its analogues by suitably modifying the amino acid sequence and studying the conformation of the synthesized compounds and the structureactivity relationship.