Yao Lin

Nature's fibrous proteins, such as α-keratin, achieve remarkable mechanical properties by undergoing strain-induced α-to-β conformational transitions. Inspired by these materials, we report a strategy for designing synthetic polypeptides that undergo similar transformations at elevated temperatures far exceeding keratin's operational range. By employing helix-confined ring-opening polymerization (ROP) of N-carboxyanhydrides (NCAs) initiated by a short poly(γ-benzyl-l-glutamate) (PBLG) precursor, we synthesized poly(O-benzyl-l-serine) (PBLS) chains that adopt an α-helical structure yet transition into β-sheets upon heating. Compression molding at carefully chosen temperatures drives PBLS segments into an α-β intermediate state, characterized by relaxed intrachain hydrogen bonds and a hexagonal packing arrangement. Under mechanical strain, these intermediate states convert in situ into β-sheets, producing significant strain-hardening well below the spontaneous α-to-β temperature threshold. This approach extends to polypeptides bearing different side chains, such as poly(S-benzyl-l-cysteine), demonstrating robust mechanical reinforcement across a wide temperature window up to ∼ 200 °C. In situ synchrotron X-ray analysis confirms that chain alignment, β-sheet formation, and domain growth occur stepwise during deformation. By harnessing the intermediate states and the supramolecular cooperativity conferred by compression-molded films, our method provides a versatile platform for developing next-generation polypeptide materials with tunable mechanical resilience and responsiveness─surpassing the temperature limitations of natural fibrous proteins and enabling potential applications demanding broad-temperature mechanical adaptability.

Helical-helical polypeptide polymerized ionic liquid block copolymers (PPIL BCPs) are synthesized to investigate the role of helical structure on self-assembly and ionic conductivity. PPIL BCPs, consisting of a cationic polypeptide (PTPLG) with bis(trifluoromethane sulfonimide) (TFSI) counterion and varying lengths connected to a length-fixed neutral poly-(γ-benzyl-_L-glutamate) (PBLG) block, exhibit stable helical conformations with minimal glass transition (T_g) variation. Here, we show that increasing PIL composition leads to a transition from poorly ordered to highly ordered lamellar (LAM) structures with the highest PIL content BCP forming a bilayer LAM structure with close-packed helices. This morphology yields a 1.5 order of magnitude higher T_g- and volume fraction-normalized ionic conductivity and a morphology factor f > 0.8 compared to less ordered BCPs with f < 0.05 and f = 2/3 for ideal lamellae. These results highlight the critical role of helical structure in optimizing ion transport, offering a design strategy for high-performance solid electrolytes.

Poly-L-hydroxyproline (PHyp) represents an important model for comprehending polyproline II helix and a key step toward mimicking collagen, the most abundant protein for animals, and holds immense potential for broad biomedical applications. The synthesis of PHyp, however, involves inefficient protection-deprotection steps and has been restricted to relatively low molecular weight (MW) and linear topology. Here, we report the first ring-opening polymerization (ROP) of unprotected hydroxyproline N-carboxyanhydrides (Hyp-NCA) for the facile one-step synthesis of PHyp with tunable linear or branching topologies. Employing an innovative water-assisted ultrafast polymerization technique, the research achieves the synthesis of linear PHyp with MW up to 11.0 kDa, featuring adjustable terminal groups and narrow dispersity. The study further introduces a tertiary amine-triggered one-pot polymerization method in DMSO, which leads to the facile preparation of branched PHyp (B-PHyp) within 2 h with MW up to 438 kDa, ~40 times higher than previous record of PHyp. Experimental and computational studies collectively uncovered novel details about the initiation, branching, and propagation steps of the reaction, providing fresh insights into the general mechanism regarding the ROP of NCA. Facile post-polymerization modification of B-PHyp affords injectable hydrogels with a critical gelization concentration as low as 1.0%. The polymers, characterized by their distinctive collagen-like polyproline type II (PPII) helices, offer significant prospects in drug delivery, wound healing, and other biomedical applications.

Spider silk, known for its exceptional tensile strength, extensibility, and toughness, continues to inspire advancements in polymer and materials science. Despite extensive research, synthesizing materials that encompass all these properties remains a significant challenge. This study addresses this challenge by developing high molecular-weight multiblock synthetic copolypeptides that mimic the hierarchical structure and mechanical properties of spider silk. Using autoaccelerated ring-opening polymerization of N-carboxyanhydrides, we synthesized copolypeptides featuring transformable β-sheet blocks. These blocks retain a helical structure during synthesis but transition into β-sheet nanocrystals in situ during solvent-free thermal mechanical processing. Compression molding was employed to induce hierarchical ordering within the copolypeptide films, resulting in a solid "liquid crystalline" structure that undergoes a temperature-induced α-to-β structural transformation. This transformation integrates β-sheet nanocrystals throughout the helical block matrix, significantly enhancing the material's mechanical performance. Our innovative synthesis and processing strategy, which involves alternating sequences of α-helical and β-sheet blocks with various β-sheet-forming NCAs, enables the customization of diverse mechanical characteristics. These advancements not only deepen our understanding of the fundamental design principles of spider silk but also pave the way for a new generation of high-performance, silk-inspired synthetic copolypeptides with broad application potential.

We report a new design of polymer phenylacetylene (PA) ligands and the ligand exchange methodology for colloidal noble metal nanoparticles (NPs). PA-terminated poly(ethylene glycol) (PEG) can bind to metal NPs through acetylide (M-C=C-R) that affords a high grafting density. The ligand-metal interaction can be switched between sigma bonding and extended pi backbonding by changing grafting conditions. The sigma bonding of PEG-PA with NPs is strong and it can compete with other capping ligands including thiols, while the pi backbonding is much weaker. The sigma bonding is also demonstrated to improve the catalytic performance of Pd for ethanol oxidation and prevent surface absorption of the reaction intermediates. Those unique binding characteristics will enrich the toolbox in the control of colloidal surface chemistry and their applications using polymer ligands.

The biological significance of self-assembled protein filament networks and their unique mechanical properties have sparked interest in the development of synthetic filament networks that mimic these attributes. Building on the recent advancement of autoaccelerated ring-opening polymerization of amino acid N-carboxyanhydrides (NCAs), this study strategically explores a series of random copolymers comprising multiple amino acids, aiming to elucidate the core principles governing gelation pathways of these purpose-designed copolypeptides. Utilizing glutamate (Glu) as the primary component of copolypeptides, two targeted pathways were pursued: first, achieving a fast fibrillation rate with lower interaction potential using serine (Ser) as a comonomer, facilitating the creation of homogeneous fibril networks; and second, creating more rigid networks of fibril clusters by incorporating alanine (Ala) and valine (Val) as comonomers. The selection of amino acids played a pivotal role in steering both the morphology of fibril superstructures and their assembly kinetics, subsequently determining their potential to form sample-spanning networks. Importantly, the viscoelastic properties of the resulting supramolecular hydrogels can be tailored according to the specific copolypeptide composition through modulations in filament densities and lengths. The findings enhance our understanding of directed self-assembly in high molecular weight synthetic copolypeptides, offering valuable insights for the development of synthetic fibrous networks and biomimetic supramolecular materials with custom-designed properties.

Control of interparticle interactions in terms of their direction and strength highly relies on the use of anisotropic ligand grafting on nanoparticle (NP) building blocks. We report a ligand deficiency exchange strategy to achieve site-specific polymer grafting of gold nanorods (AuNRs). Patchy AuNRs with controllable surface coverage can be obtained during ligand exchange with a hydrophobic polystyrene ligand and an amphiphilic surfactant while adjusting the ligand concentration (C_PS) and solvent condition (C_water in dimethylformamide). At a low grafting density of ≤0.08 chains/nm², dumbbell-like AuNRs with two polymer domains capped at the two ends can be synthesized through surface dewetting with a high purity of >94%. These site-specifically-modified AuNRs exhibit great colloidal stability in aqueous solution. Dumbbell-like AuNRs can further undergo supracolloidal polymerization upon thermal annealing to form one-dimensional plasmon chains of AuNRs. Such supracolloidal polymerization follows the temperature-solvent superposition principle as revealed by kinetic studies. Using the copolymerization of two AuNRs with different aspect ratios, we demonstrate the design of chain architectures by varying the reactivity of nanorod building blocks. Our results provide insights into the postsynthetic design of anisotropic NPs that potentially serve as units for polymer-guided supracolloidal self-assembly.