Scholarlink

<p>Nature achieves extraordinary mechanical performance by precisely regulating β-structure formation in proteins such as fibroin, elastin, and resilin. Replicating this level of structural control remains a major challenge in protein engineering. Here, we integrate biomimetic design with deep learning–guided de novo protein engineering to create environmentally responsive β-hairpin peptides. Computational optimization enhanced β-hairpin propensity, hydrophilicity, and solvent accessibility while preserving high aqueous solubility. The peptides remain intrinsically disordered in solution but rapidly undergo a β-hairpin transition upon exposure to minimal concentrations of sodium dodecyl sulfate (SDS), a model amphiphilic trigger. This structural conversion drives assembly into mechanically reinforced materials exhibiting increased stiffness and hardness relative to the unfolded state. Our findings provide mechanistic insight into regulated β-structure formation and demonstrate a scalable strategy for programming environmentally triggered protein folding, hierarchical assembly, and mechanical function, opening new opportunities for the rational design of next-generation adaptive biomaterials.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Designed β-hairpin switches for controllable mechanical properties

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年7月20日

查看全文
  • Gabriela Wojtan,
  • Sofia Julin,
  • Robert Pylkkänen,
  • Navneet Dwivedi,
  • Cajsa Malm,
  • Anna Borisova,
  • Timo Laakko,
  • Marc Baldus,
  • Piotr Batys,
  • Pezhman Mohammadi

摘要

Nature achieves extraordinary mechanical performance by precisely regulating β-structure formation in proteins such as fibroin, elastin, and resilin. Replicating this level of structural control remains a major challenge in protein engineering. Here, we integrate biomimetic design with deep learning–guided de novo protein engineering to create environmentally responsive β-hairpin peptides. Computational optimization enhanced β-hairpin propensity, hydrophilicity, and solvent accessibility while preserving high aqueous solubility. The peptides remain intrinsically disordered in solution but rapidly undergo a β-hairpin transition upon exposure to minimal concentrations of sodium dodecyl sulfate (SDS), a model amphiphilic trigger. This structural conversion drives assembly into mechanically reinforced materials exhibiting increased stiffness and hardness relative to the unfolded state. Our findings provide mechanistic insight into regulated β-structure formation and demonstrate a scalable strategy for programming environmentally triggered protein folding, hierarchical assembly, and mechanical function, opening new opportunities for the rational design of next-generation adaptive biomaterials.