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Background <p>The α-helix, a fundamental and highly versatile secondary structure in proteins, holds substantial promise in biomedicine owing to its characteristic right-handed helical conformation, regular hydrogen-bonding network, and predictable side-chain arrangement.</p> Main body <p>This review systematically outlines the structural features and stabilization mechanisms of α-helical peptides, along with core strategies in drug design, including solid-phase peptide synthesis (SPPS), ring-opening polymerization (ROP) of <i>N</i>-carboxyanhydrides (NCAs), conformational stapling, non-natural amino acid incorporation, and stimuli-responsive modifications. We also highlight frontier advances in computational simulation and deep-learning approaches for <i>de novo</i> structural prediction and functional optimization. Regarding applications, this review elaborates on the mechanisms and recent progress of α-helical peptides in antimicrobial and anticancer therapies, immunomodulation, and tissue engineering, covering membrane-targeting mechanisms, immune cell modulation, vaccine design, drug delivery systems, and bioactive regenerative scaffolds.</p> Conclusions <p>Despite their superior biocompatibility, functional programmability, and translational potential of α-helical peptides, challenges remain including in vivo stability, scalable manufacturing, and optimizing pharmacokinetics. Future advances driven by multidisciplinary integration and artificial intelligence (AI)-guided design are expected to further enable α-helical peptides as pivotal tools in precision and regenerative medicine.</p>

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α-Helical peptides: design strategies and recent advances in biomedical applications

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年4月20日

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  • Mengyuan Yin,
  • Fei Ding,
  • Guanghua Luo,
  • Miaomei Yu

摘要

Background

The α-helix, a fundamental and highly versatile secondary structure in proteins, holds substantial promise in biomedicine owing to its characteristic right-handed helical conformation, regular hydrogen-bonding network, and predictable side-chain arrangement.

Main body

This review systematically outlines the structural features and stabilization mechanisms of α-helical peptides, along with core strategies in drug design, including solid-phase peptide synthesis (SPPS), ring-opening polymerization (ROP) of N-carboxyanhydrides (NCAs), conformational stapling, non-natural amino acid incorporation, and stimuli-responsive modifications. We also highlight frontier advances in computational simulation and deep-learning approaches for de novo structural prediction and functional optimization. Regarding applications, this review elaborates on the mechanisms and recent progress of α-helical peptides in antimicrobial and anticancer therapies, immunomodulation, and tissue engineering, covering membrane-targeting mechanisms, immune cell modulation, vaccine design, drug delivery systems, and bioactive regenerative scaffolds.

Conclusions

Despite their superior biocompatibility, functional programmability, and translational potential of α-helical peptides, challenges remain including in vivo stability, scalable manufacturing, and optimizing pharmacokinetics. Future advances driven by multidisciplinary integration and artificial intelligence (AI)-guided design are expected to further enable α-helical peptides as pivotal tools in precision and regenerative medicine.