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<p>Antimicrobial peptides (AMPs) represent a promising class of alternatives to conventional antibiotics. In this study, we compared the structural and functional properties of three synthetic undecapeptides: the anionic <b>Cn-AMP2</b> and its N-terminally acetylated derivative (<b>Ac-CnAMP2</b>), versus the cationic α-helical peptide <b>BP52</b>. While <b>BP52</b> exhibited strong antibacterial activity against both Gram-positive and Gram-negative bacteria, <b>Cn-AMP2</b> and <b>Ac-CnAMP2</b> showed no measurable antibacterial effects up to 128µM. Hemolysis assays revealed that <b>BP52</b> caused mild to moderate lysis of red blood cells, whereas the anionic peptides were non-hemolytic. Molecular dynamics simulations confirmed the enhanced membrane insertion, clustering behavior, and bilayer disruption induced by <b>BP52</b>, in contrast to the limited interaction profiles of <b>Cn-AMP2</b>. These findings underscore the importance of positive charge, helical conformation, and amphipathic topology in driving membrane action and offer insights for designing optimized AMP-based therapeutics.</p> Graphic Abstract <p></p>

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Structure–Function Insights into Anionic and Cationic Undecapeptides: A Combined Modeling and Antibacterial Study

  • 期刊论文

  • 发表日期：

    2026年5月20日

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  • Thang Nguyen Quoc,
  • Hai Bui Thi Phuong,
  • Duc Nguyen Van,
  • Duc Nguyen Minh,
  • Hoang Vu Dinh,
  • Tung Truong Thanh,
  • Huy Luong Xuan

摘要

Antimicrobial peptides (AMPs) represent a promising class of alternatives to conventional antibiotics. In this study, we compared the structural and functional properties of three synthetic undecapeptides: the anionic Cn-AMP2 and its N-terminally acetylated derivative (Ac-CnAMP2), versus the cationic α-helical peptide BP52. While BP52 exhibited strong antibacterial activity against both Gram-positive and Gram-negative bacteria, Cn-AMP2 and Ac-CnAMP2 showed no measurable antibacterial effects up to 128µM. Hemolysis assays revealed that BP52 caused mild to moderate lysis of red blood cells, whereas the anionic peptides were non-hemolytic. Molecular dynamics simulations confirmed the enhanced membrane insertion, clustering behavior, and bilayer disruption induced by BP52, in contrast to the limited interaction profiles of Cn-AMP2. These findings underscore the importance of positive charge, helical conformation, and amphipathic topology in driving membrane action and offer insights for designing optimized AMP-based therapeutics.

Graphic Abstract