Research
Precise Synthesis of Functional Protein-Mimetic Peptides
Protein-mimetic peptides are macromolecules with designed sequences that mimic the conformations, assembly behavior and biological functions of natural structural proteins. Their biocompatibility, design flexibility and dynamic responsiveness make them key building blocks for biomedical polymer materials. Alongside traditional microbial fermentation approaches using organisms such as E. coli, we develop precise, fully chemical synthesis strategies to overcome limitations of biosynthesis and control amino acid sequence, chirality and topology. We aim to establish proprietary peptide synthesis technologies for next-generation biomedical polymer materials.
Assembly and Condensation of Intrinsically Disordered Proteins
Intrinsically disordered proteins function without adopting stable three-dimensional folds. Their conformational flexibility and environmental responsiveness enable assembly and condensation through liquid–liquid phase separation, making them both important biological components and models for protein-mimetic peptides and dynamic biomedical materials. We investigate how sequence, assembly and condensation determine conformational dynamics, biological function and hierarchical organization. Combined with precise synthesis, this knowledge guides the design of responsive, biocompatible peptides for tissue regeneration and repair and targeted drug delivery.
Clinically Oriented Supramolecular Drug Design and Biomedical Applications
Drug molecules are not only functional units that exert pharmacological activity; through non-covalent intermolecular interactions they can also form supramolecular materials with defined structures and functions. By designing and tuning the hydrophilic–hydrophobic balance, π–π stacking, hydrogen bonding, electrostatic interactions and multicomponent cooperation of prodrug molecules, we drive their assembly into nanofibers, hydrogels and liquid biomolecular condensates, restructuring "single-molecule drugs" into "supramolecular drugs" and offering a new paradigm beyond conventional carrier-based drug delivery. We study the supramolecular self-assembly, co-assembly and liquid–liquid phase separation of prodrugs, linking molecular structure, supramolecular behavior and dynamic transitions, and revealing how different condensed-state structures govern drug delivery, cell interactions and therapeutic outcomes. Building on this, we combine prodrug design, cooperative assembly with functional peptides and programmable peptide engineering to create supramolecular drug systems with high drug loading, minimal excipients, local retention, sustained release and environmental responsiveness, and extend them to biomedical applications in cancer, infection, inflammation and ophthalmic diseases, providing new molecular design strategies and material foundations for clinically oriented drug delivery.
Acknowledgements致谢
We gratefully acknowledge the following programs and agencies for supporting our research.
