Ultrastable de novo SuperMyo proteins enable high-performance macroscopic fibers from minimal repeats

Conventional routes to strong protein fibers rely on the assembly of high-molecular-weight polymers, where mechanical performance is achieved by increasing the number of tandem repeats within the polypeptide chain. This repeat-number strategy inherently complicates production and limits scalability. Here, we introduce a contrasting paradigm in which macroscopic strength is derived not from chain length, but from the increased intrinsic mechanostability of each repeating unit. We implement this using computationally designed immunoglobulin-domain-based SuperMyo proteins, whose force-bearing β-strands are engineered to form ultra-dense hydrogen-bond networks, yielding unfolding forces nearly double those of natural immunoglobulin domains at a pulling speed of 1000 nm s−1. When assembled into minimal tetrameric constructs (only four repeats), these designed units retain their high nanomechanical stability. Processed via wet-spinning, the tetramers form continuous macroscopic fibers with a tensile strength up to 372 MPa and a toughness of 61 MJ m⁻³. Crucially, this performance matches or exceeds that of previously reported fibers spun from polymers containing far more repeats (e.g., 64-mers). Structural analyses confirm that the enhanced stability of the monomers promotes superior β-sheet crystallization and alignment during fiber formation. By demonstrating that engineering the mechanical stability of protein building blocks is a potential strategy for producing strong protein fibers from low-repeat-number constructs, this work establishes a more efficient and scalable foundation for manufacturing high-performance protein-based materials. High-performance biofuels require a well-defined flash point, yet the coexistence of pentanol isomers can introduce ignition-point variations that compromise fuel performance. Here, the authors present an electrochemiluminescence shunt strategy based on a bifunctional catalytic system that exploits the distinct reactive oxygen species scavenging properties of pentanol isomers. The approach generates differential anodic and cathodic luminol signals, enabling their precise discrimination and providing a powerful tool for fuel-quality assessment

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Publication Details

Journal
Nature Communications
Published
2026-10-31
DOI
https://doi.org/10.1038/s41467-026-78574-x
Primary Topic
Silk-based biomaterials and applications
Type
article
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article

Ultrastable de novo SuperMyo proteins enable high-performance macroscopic fibers from minimal repeats

Peng Zheng, Bin Zheng, Xiaodong Han, Yuanhao Liu et al.
Nature Communications
Silk-based biomaterials and applications
article

Ultrastable de novo SuperMyo proteins enable high-performance macroscopic fibers from minimal repeats

Peng Zheng, Bin Zheng, Xiaodong Han, Yuanhao Liu, Shengbang Xu, Juanjuan Su, Jingjing Li
article en

Abstract

Conventional routes to strong protein fibers rely on the assembly of high-molecular-weight polymers, where mechanical performance is achieved by increasing the number of tandem repeats within the polypeptide chain. This repeat-number strategy inherently complicates production and limits scalability. Here, we introduce a contrasting paradigm in which macroscopic strength is derived not from chain length, but from the increased intrinsic mechanostability of each repeating unit. We implement this using computationally designed immunoglobulin-domain-based SuperMyo proteins, whose force-bearing β-strands are engineered to form ultra-dense hydrogen-bond networks, yielding unfolding forces nearly double those of natural immunoglobulin domains at a pulling speed of 1000 nm s−1. When assembled into minimal tetrameric constructs (only four repeats), these designed units retain their high nanomechanical stability. Processed via wet-spinning, the tetramers form continuous macroscopic fibers with a tensile strength up to 372 MPa and a toughness of 61 MJ m⁻³. Crucially, this performance matches or exceeds that of previously reported fibers spun from polymers containing far more repeats (e.g., 64-mers). Structural analyses confirm that the enhanced stability of the monomers promotes superior β-sheet crystallization and alignment during fiber formation. By demonstrating that engineering the mechanical stability of protein building blocks is a potential strategy for producing strong protein fibers from low-repeat-number constructs, this work establishes a more efficient and scalable foundation for manufacturing high-performance protein-based materials. High-performance biofuels require a well-defined flash point, yet the coexistence of pentanol isomers can introduce ignition-point variations that compromise fuel performance. Here, the authors present an electrochemiluminescence shunt strategy based on a bifunctional catalytic system that exploits the distinct reactive oxygen species scavenging properties of pentanol isomers. The approach generates differential anodic and cathodic luminol signals, enabling their precise discrimination and providing a powerful tool for fuel-quality assessment

Nature Communications
Chinese Academy of Sciences (CN), Changchun Institute of Applied Chemistry (CN), Nanjing Drum Tower Hospital (CN), University of Chinese Academy of Sciences (CN), Nanjing University (CN)
Openalex Percentile: Top 28%
Silk-based biomaterials and applications
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