Dynamic Peptide Nanoframework-Guided Protein Coassembly: Advancing Adhesion Performance with Hierarchical Structures.

Hierarchical structures are essential in natural adhesion systems. Replicating these in synthetic adhesives is challenging due to intricate molecular mechanisms and multiscale processes. Here, we report three phosphorylated peptides featuring a hydrophobic self-assembly motif linked to a hydrophilic phosphorylated sequence (pSGSS), forming peptide fibril nanoframeworks. These nanoframeworks effectively coassemble with elastin-derived positively charged proteins (PCP), resulting in complex coacervate-based adhesives with hierarchical structures. Our method enables the controlled regulation of both cohesion and adhesion properties in the adhesives. Notably, the complex adhesives formed by the dityrosine-containing peptide and PCP demonstrate an exceptional interfacial adhesion strength of up to 30 MPa, outperforming most known supramolecular adhesives and rivaling cross-linked chemical adhesives. Additionally, these adhesives show promising biocompatibility and bioactivity, making them suitable for applications such as visceral hemostasis and tissue repair. Our findings highlight the utility of bioinspired hierarchical assembly combined with bioengineering techniques in advancing biomedical adhesives.