Hierarchical Engineering of Amphiphilic Peptides Nanofibrous Crosslinkers toward Mechanically Robust, Functionally Customable, and Sustainable Supramolecular Hydrogels

Abstract Hierarchical architectures spanning multiple length scales are ubiquitous in biological tissues, conferring them with both mechanical robustness and dynamic functionalities via structural reorganization under loads. The design of hierarchical architectures within synthetic hydrogels to concurrently achieve mechanical reinforcement and functional integration remains challenging. Here, a biomimetic hierarchical engineering approach is reported to develop mechanically robust and function‐customizable supramolecular hydrogels by utilizing strong yet dynamic fibrous nanoarchitectures of amphiphilic peptides as crosslinkers. This design, on one hand, resolves the strength‐toughness trade‐off in hydrogel design through energy‐dissipative mechanisms involving dynamic detachment and reinsertion of peptides within their assembled nanostructures upon loading. On the other hand, the amphiphilicity and sequence programmability of peptides allow spatially orthogonal integration of multiple dynamic functionalities across distinct structural domains, including lipophilic fluorophore encapsulation, photopatterning capability, and anisotropic contraction. Capitalizing on its ultralow hysteresis and rapid recovery properties, the hydrogel's effectiveness is demonstrated as high‐sensitivity strain sensors. Moreover, the fully noncovalent crosslinking strategy permits closed‐loop recycling and reprocessing via reversible crosslinker disassembly‐reassembly processes. Through systematic extension of this principle across diverse peptide systems, a generalized platform is demonstrated for creating advanced soft materials that synergistically integrate traditionally incompatible attributes of mechanical robustness, customable dynamic functionality, and environmental sustainability.