Dynamic\nPeptide Nanoframework-Guided Protein Coassembly:\nAdvancing Adhesion Performance with Hierarchical Structures

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