Yunpeng Wang,Wei Liao,Jiahao Sun,Rajib Nandi,Zhongqiang Yang
Human muscles, including skeletal, smooth, and cardiac muscles, are able to perform diverse deformations and execute complex biofunctions stimulated by nerve signals. Similarly, liquid crystal elastomer (LCE), which can respond to external stimuli with large and reversible deformations, demonstrates superior advantages to mimic nature muscles to fabricate artificial muscles. Till now, LCE has been utilized to simulate deformations and related functions of skeletal and smooth muscles. However, limited by the existing fabrication strategy, employing LCE to mimic the motion of cardiac muscles and further realizing the structure-determined pumping functions, is still an open challenge. Learning from the specific spatial arrangements and synergistic actuation of cardiac muscle fibers within human heart, a simple and general strategy to construct artificial cardiac muscles with LCE fibers is proposed. In this work, LCE fibers with similar modulus and actuation behavior to muscle fibers are fabricated and spatially arranged in biological architectures as cardiac muscle fibers. As a result, artificial cardiac muscles are constructed and are able to perform simultaneous contraction and torsion motions, realizing heart-pumping functions. This general strategy should be also applicable for other smart materials to conduct challenging tasks.
Wenzhe Zhang,Ying Wan,Chaoyi Xue,Zhengxing Chen,Ren Wang,Wei Feng,Yanan Li,Tao Wang
Multicompartmented nanostructures, which mirror the complexity of living cells, are promising for bio-related applications. However, controlling the spatial arrangement within natural biopolymer assemblies, like protein nanoparticles, is challenging. In our study, we reveal a facile method for compartmentalizing the interiors of protein nanoparticles by co-assembling rice proteins (RPs) and soy protein isolates (SPIs) through simultaneous folding. The assembly of these two protein types results in nanoparticles with a hydrophobic core to accommodate hydrophobic substances, such as eugenol, leading to its internalization. The protein–ligand (SPI-eugenol) interaction then triggers SPI gelation within the nanoparticle cores, forming distinct physical barriers hindering the complete merging of eugenol droplets. Subsequent dialysis of the nanoparticles containing eugenol against water facilitated the removal of eugenol. This step was crucial for forming multicompartmented nanoparticles (MCNPs) with adjustable interior complexities, including varying numbers of compartments and different hollowing rates related to various SPI:RP mass ratios. This allows us to endow MCNPs with adjustable barrier effects tailoring controllable responses of the encapsulated payload, vitamin D 3 (VD 3 ), under different physicochemical conditions. Our study demonstrates a straightforward method for constructing biomacromolecular architectures with precise control over their compartmentalization.
Nanozymes are nanomaterials designed to mimic the catalytic functions of natural enzymes, offering advantages such as enhanced stability, tunability, and scalability. Although precise control over the spatial arrangement of catalytic centers is essential for maximizing nanozyme activity, it remains a fundamental challenge in nanozyme design. Here, we present a supramolecular strategy to achieve molecular-level engineering of catalytic centers by grafting hemin onto monodisperse cellulose oligomers (MCOs). The crystallization-driven self-assembly of MCOs directs the spatial organization of hemin while preventing its detrimental aggregation. Systematically tuning of the cellulose chain length reveals that a degree of polymerization (DP) of 6 optimally balances supramolecular packing and increased availability of active sites, whereas shorter (DP1) and longer (DP20) chains compromise catalytic performance due to aggregation or decreased substrate binding affinity. Structural analyses reveal that chain-length-directed crystallization governs nanozyme morphology, aggregation behavior, and catalytic performance. Through this approach, we achieve an approximately 500-fold enhancement in catalytic efficiency over free hemin, while structural analyses elucidate the role of chain-length-dependent crystallization in governing nanozyme morphology and performance. This study establishes transferable cellulose-based supramolecular strategy for engineering high-performance nanozymes with broad applicability across diverse catalytic systems.
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