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| Main Authors: | , , , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Acta biomaterialia
2026
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/42134754/ |
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Table of Contents:
- Tyrosine-driven hierarchical self-assembly unlocks robust non-Dopa wet adsorption in marine adhesive protein. Wang, Lulu Zheng, Zhanghui Liao, Zhenyu Zhang, Pu Yang, Juan Wei, Hongyu Yan, Jicheng Chu, Xiangqiang Fan, Jun Liu, Weizhi Tyrosine Adsorption Animals Molecular Dynamics Simulation Dihydroxyphenylalanine Antioxidants Wettability Proteins Many marine sessile organisms achieve robust underwater adsorption through 3,4-dihydroxyphenylalanine (Dopa)-independent strategies, yet the underlying self-assembly mechanisms remain elusive. Here, we decipher the Ca-triggered interfacial adsorption of a sea anemone thrombospondin-1 type I repeat-like (TSRL) protein, identifying its tyrosine-rich T3 subunit as the core mediator for coating formation. The fabricated T3 coatings exhibited strong wet adsorption stability, biocompatibility, and intrinsic antioxidant activity. Mechanistically, T3 self-assembly is driven by favorable enthalpy, initiating with nanosphere aggregation and forming hierarchical fishnet-like microstructures. Molecular dynamics simulations revealed that, unlike the rapid collisions of T1 subunit, the slower diffusion of T3 enables precise orientation and pairing, leading to a marked increase in inter-residue contacts dominated by cation-π interactions between lysine and tyrosine residues, alongside π-π stacking. Mutant studies confirm that disrupting these interactions impairs both self-assembly and interfacial adsorption, establishing positioned tyrosine residues as molecular stickers. Together, these findings establish a tyrosine-mediated, non-Dopa marine adsorption paradigm and highlight the T3 protein as a promising biomaterial platform for tissue engineering and antioxidant biomedical applications. STATEMENT OF SIGNIFICANCE: This work reports a tyrosine-driven, Dopa-independent wet adsorption paradigm in marine biological systems, fundamentally expanding the current understanding of underwater adsorption mechanisms. The discovery that precisely positioned tyrosine residues can orchestrate hierarchical self-assembly through specific π-π and cation-π interactions establishes a new conceptual framework for designing bioinspired coatings. Beyond its fundamental implications, this system offers a versatile combination of robust wet adsorption and inherent biocompatibility, addressing a critical challenge in biomedical adhesive development. Moreover, the intrinsic reactive oxygen species (ROS)-scavenging capacity positions this protein-based platform as a multifunctional biomaterial with promising applications in wound healing, tissue engineering, and antioxidant therapeutics.