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Introduction <p>The antibacterial, anti-biofilm, and hemolytic activities of five synthetic analogs of Anoplin, Temporin, and Aurein were evaluated.</p> Methods <p>Five 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.</p> Results <p>The 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&#xa0;µg/mL. Antibiofilm activity was evaluated against <i>E. coli</i> (K12), <i>P. aeruginosa</i> (PA01), and <i>S. aureus</i> (SH1000) reference strains.</p> Conclusions <p>The peptide demonstrating the most significant antibiofilm activity was Anoplin_k1 (≤ 64&#xa0;µg/mL), whereas the Aurein derivatives exhibited reduced antibiofilm activity.</p>

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Antimicrobial and Antibiofilm Activity of Analogous Synthetic Peptides from Anoplin, Temporin, and Aurein

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年1月23日

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  • Kevin Cruz Orozco,
  • Marco Antonio Ibarra Valencia,
  • Humberto Barrios Camacho,
  • Gerardo Corzo Burguete,
  • Iván Arenas Sosa

摘要

Introduction

The antibacterial, anti-biofilm, and hemolytic activities of five synthetic analogs of Anoplin, Temporin, and Aurein were evaluated.

Methods

Five 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.

Results

The 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.

Conclusions

The peptide demonstrating the most significant antibiofilm activity was Anoplin_k1 (≤ 64 µg/mL), whereas the Aurein derivatives exhibited reduced antibiofilm activity.