Cofactor-free oxidase-mimetic nanomaterials from self-assembled histidine-rich peptides

Liu, Qing; Wan, Kaiwei; Shang, Yingxu; Wang, Zhen‐Gang; Zhang, Yiyang; Dai, Luru; Wang, Chen; Wang, Hui; Shi, Xinghua; Li, Dongsheng; Ding, Baoquan

doi:10.1038/s41563-020-00856-6

Cited by 96 publications

(73 citation statements)

References 50 publications

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“…In the case of oPD oxidation promoted by VHVHVQV we observed at least two catalyst turnovers (Figure S13, Supporting Information) with maximum catalytic efficiencies reaching 0.45 m −1 s −1 (Table 3) making it the first example of catalytic oxidation of an organic substrate promoted by peptide assemblies. Just like Liu et al [15] . we observed ≈20 % turnover in the case of TMB.…”

Section: Methodssupporting

confidence: 88%

“…While this paper was in review, Liu et al. reported the co‐factor‐free oxidation of TMB promoted by assemblies formed by histidine oligomer H15, however no catalyst turnover was reported (product/catalyst ratio of less than 20 %) [15] . In the case of oPD oxidation promoted by VHVHVQV we observed at least two catalyst turnovers (Figure S13, Supporting Information) with maximum catalytic efficiencies reaching 0.45 m −1 s −1 (Table 3) making it the first example of catalytic oxidation of an organic substrate promoted by peptide assemblies.…”

Section: Methodsmentioning

confidence: 88%

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Self‐Assembling Catalytic Peptide Nanomaterials Capable of Highly Efficient Peroxidase Activity

Zozulia

Marshall

Kim

et al. 2021

Chemistry A European J

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The self‐assembly of short peptides gives rise to versatile nanomaterials capable of promoting efficient catalysis. We have shown that short, seven‐residue peptides bind hemin to produce functional catalytic materials which display highly efficient peroxidation activity, reaching a catalytic efficiency of 3×105 m−1 s−1. Self‐assembly is essential for catalysis as non‐assembling controls show no activity. We have also observed peroxidase activity even in the absence of hemin, suggesting the potential to alter redox properties of substrates upon association with the assemblies. These results demonstrate the practical utility of self‐assembled peptides in various catalytic applications and further support the evolutionary link between amyloids and modern‐day enzymes.

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Section: Methodssupporting

confidence: 88%

Section: Methodsmentioning

confidence: 88%

Self‐Assembling Catalytic Peptide Nanomaterials Capable of Highly Efficient Peroxidase Activity

Zozulia

Marshall

Kim

et al. 2021

Chemistry A European J

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“…In rPN, each end of the PN has 18 histidine residues consisting of three His-tag fragments (Figure 1b). Since histidine-rich peptides can self-assemble in solution via non-covalent bonds in the absence of metal ions, [27][28][29] rPN is expected to form multipoint interactions. In contrast, rPN_ΔHis will not form specific intermolecular interactions due to the absence of His-tag fragments (Figure 1c).…”

Section: Molecular Designmentioning

confidence: 99%

Protein Needles Designed to Self‐Assemble through Needle Tip Engineering

Kikuchi

Fukuyama

Uchihashi

et al. 2022

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The dynamic process of formation of protein assemblies is essential to form highly ordered structures in biological systems. Advances in structural and synthetic biology have led to the construction of artificial protein assemblies. However, development of design strategies exploiting the anisotropic shape of building blocks of protein assemblies has not yet been achieved. Here, the 2D assembly pattern of protein needles (PNs) is controlled by regulating their tip‐to‐tip interactions. The PN is an anisotropic needle‐shaped protein composed of β‐helix, foldon, and His‐tag. Three different types of tip‐modified PNs are designed by deleting the His‐tag and foldon to change the protein–protein interactions. Observing their assembly by high‐speed atomic force microscopy (HS‐AFM) reveals that PN, His‐tag deleted PN, and His‐tag and foldon deleted PN form triangular lattices, the monomeric state with nematic order, and fiber assemblies, respectively, on a mica surface. Their assembly dynamics are observed by HS‐AFM and analyzed by the theoretical models. Monte Carlo (MC) simulations indicate that the mica‐PN interactions and the flexible and multipoint His‐tag interactions cooperatively guide the formation of the triangular lattice. This work is expected to provide a new strategy for constructing supramolecular protein architectures by controlling directional interactions of anisotropic shaped proteins.

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“…Since the discovery of Fe 3 O 4 nanoparticles with peroxidase-like activity, [1] many nanomaterials,t ermed as nanozymes,s uch as noble metals, [2] metal oxides, [3] 2D matters, [4] nanocarbon, [5] and self-assembled peptides [6] have been developed for mimicking enzyme-like functions.T hese nanozymes are low-cost, high-stable,a nd mass-produced, [7] which well surmount natural enzymes weakness,t hus gaining diverse applications ranging from biosensing, [8] disease therapy, [5a, 9] to drug-drug interaction studies. [10] Nonetheless,a s the lack of enzyme-like molecular recognition units,t he intrinsic reaction selectivity of nanozymes is poor,t hereby hindering more high demanding applications.…”

Section: Introductionmentioning

confidence: 99%

Cascaded Nanozyme System with High Reaction Selectivity by Substrate Screening and Channeling in a Microfluidic Device**

et al. 2021

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Surpassing natural enzymes in cost, stability and mass production, nanozymes have attracted wide attention in fields from disease diagnosis to tumor therapy. However, nanozymes intrinsically have lowr eaction selectivity,w hich significantly restricts their applications.Ageneral method is reported to address this challenge by following ab iomimetic operation principle of substrates channeling and screening. Tw oo xidase-and peroxidase-like nanozymes (i.e., emerging N-doped carbon nanocages and Prussian blue nanoparticles), were cascaded as ap roof of concept to improve the reaction selectivity in transforming the substrate into the targeted product by more than 2000 times.T he cascaded nanozymes were also adopted to as patially confined microfluidic device, leading to more than 100-fold enhancement of the reaction efficiency due to signal amplification.

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Cofactor-free oxidase-mimetic nanomaterials from self-assembled histidine-rich peptides

Cited by 96 publications

References 50 publications

Self‐Assembling Catalytic Peptide Nanomaterials Capable of Highly Efficient Peroxidase Activity

Self‐Assembling Catalytic Peptide Nanomaterials Capable of Highly Efficient Peroxidase Activity

Protein Needles Designed to Self‐Assemble through Needle Tip Engineering

Cascaded Nanozyme System with High Reaction Selectivity by Substrate Screening and Channeling in a Microfluidic Device**

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