Abstract
IntroductionThe antibacterial, anti-biofilm, and hemolytic activities of five synthetic analogs of Anoplin, Temporin, and Aurein were evaluated.MethodsFive peptides, varying in length from ten to thirteen amino acids, were chemically synthesized to preserve the physicochemical characteristics inherent to the original antimicrobial peptides. These characteristics included the hydrophobic ratio, Boman index, GRAVY, stability index, and aliphatic index, with the additional objective of enhancing their antimicrobial effectiveness.ResultsThe most promising peptides were derived from Anoplin, particularly Anoplin_k1, which was identified as the most hydrophobic peptide with a net charge of + 2; however, it exhibited slightly increased hemolytic activity compared to the other four peptides. Anoplin_k1 demonstrated efficacy that was comparable to reference strains as well as against clinically isolated bacterial strains. The synthetic peptide Temporin ALk_k3, an analog of Temporin Alk, did not show antimicrobial activity above 100 µg/mL. Antibiofilm activity was evaluated against E. coli (K12), P. aeruginosa (PA01), and S. aureus (SH1000) reference strains.ConclusionsThe peptide demonstrating the most significant antibiofilm activity was Anoplin_k1 (≤ 64 µg/mL), whereas the Aurein derivatives exhibited reduced antibiofilm activity.
Published Version
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