Self-assembly of fibril-forming histidine-rich peptides for cofactor-free oxidase-mimetic catalysis

Liu, Yuanxi; Du, Peidong; Teng, Qiao; Sun, Hao; Ye, XiangYu; Wang, Zhen-Gang

doi:10.1016/j.supmat.2022.100012

Cited by 15 publications

(21 citation statements)

References 27 publications

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“…Site-directed mutagenesis, which allows selective engineering of genome sequences and creates targeted mutation on proteins, is the most widely used strategy to discover the active site structures and the mechanism of the enzymatic action, as well as modification of enzymes. Site-directed mutagenesis is often accompanied by laborious high-throughput screening, the off-target mutation, and sometimes changes in the folding structures of the proteins. , Supramolecular catalysts that assembled from the catalytic species have attracted considerable attention in catalyzing reactions similar to natural enzymes. − The supramolecular catalysts have simpler structures compared to native enzymes, so the catalytic functions can be tailored by modifying any of the catalytic species (also called molecular building blocks). However, the modifications of the building blocks tend to disturb the forces that hold the building blocks, leading to the unpredictable structural changes of the supramolecular catalytic sites.…”

Section: Introductionmentioning

confidence: 99%

Enzyme-Mimicking Materials from Designed Self-Assembly of Lysine-Rich Peptides and G-Quadruplex DNA/Hemin DNAzyme: Charge Effect of the Key Residues on the Catalytic Functions

Sun

Teng

et al. 2022

Biomacromolecules

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In enzymatic active sites, the essential functional groups are spatially arranged as a result of the enzyme threedimensional folding, which leads to remarkable catalytic properties. We are inspired to self-assemble the polylysine peptides with guanine-rich DNA and hemin as cofactor to fabricate the peroxidase-mimicking catalytic nanomaterials. The DNA can fold into G-quadruplex to provide a supramolecular scaffold and a nucleobase for supporting and coordinating hemin, and the polylysine provides amine as distal groups to promote the H 2 O 2 adsorption to the iron of hemin. The polylysine and DNA components synergistically accelerated the hemin-catalyzed reactions, and the complex containing ε-polylysine exhibited higher activity than α-polylysine. This activity difference is attributed to the higher pK a value and more susceptible protonation of amine of ε-polylysine than α-polylysine. The εpolylysine/DNA/hemin had similar coordination states of hemin and conformations of the components to α-polylysine/DNA/ hemin but accelerated the formation of the intermediate compound I faster than α-polylysine. Theoretical simulation reveals that the unprotonated NH 2 behaved like a base catalyst, similar to His-42 residue in the natural heme pocket, while the protonated NH 3 + acted as an acid, which indicated that the base catalyst on the distal side of the hemin pocket is more active than the acid. This work provides an avenue to control the distribution of the catalytic residues in an enzyme-like active site and to understand the roles of the key residues of native enzymes.

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Section: Introductionmentioning

confidence: 99%

Enzyme-Mimicking Materials from Designed Self-Assembly of Lysine-Rich Peptides and G-Quadruplex DNA/Hemin DNAzyme: Charge Effect of the Key Residues on the Catalytic Functions

Sun

Teng

et al. 2022

Biomacromolecules

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“…Based on the kinetic parameters from a steady-state kinetic assay (Figures S10 and Table S1), the Fe 3+ :L-MOFs/TiNM exhibits peroxidase-mimicking catalytic activity, reflected by the catalytic oxidation of ABTS to ABTS •+ in the presence of H 2 O 2 . 36 Figure 1 shows the schematic mechanism for the inhibition effect on peroxidase-mimicking activity induced by enantiomer recognition. For Fe 3+ :L-MOFs/TiNM, the post-modified L-TA molecules on homochiral MOFs work as a chiral selector and recognizes cystine enantiomers via hydrogen bonding.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Target Recognition-Triggered Peroxidase-Mimicking Activity Depression in Homochiral Nanochannels for Identifying Cystine Enantiomers

Guo

Zhao

et al. 2023

Anal. Chem.

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Enantioselective identification of chiral molecules is of paramount importance in medical science, biochemistry, and pharmaceutics owing to the configuration-dependent activities of enantiomers. However, the identical physicochemical properties of enantiomers remain challenging in chiral sensing. In this study, inspired by the peroxidase-mimicking activity of Fe(III)-based nanomaterials, an enantioselective artificial architecture is constructed on TiO2 nanochannels. Homochiral Ti-based metal–organic frameworks (MOFs) use a 2,2′-bipyridine-5,5′-dicarboxylic acid ligand as the artificial enzyme skeleton, Fe(III) as peroxidase-mimicking centers, and l-tartaric acid (TA) as a chiral recognition selector. Using l-/d-cystine as model enantiomers, the chiral moieties of l-TA on Ti-MOFs allow stereoselective recognition of guest molecules through hydrogen bonds formed between chiral cystine and the host. In a tris(2-carboxyethyl)phosphine hydrochloride-containing environment, the disulfide bonds in cystine molecules are further cleaved, and the HS-tails react with Fe(III) active sites, causing the loss of peroxidase-like performance of nanochannels. Benefitting from the nanochannel architecture’s current–potential (I–V) properties, the selective recognition of cystine enantiomers is directly monitored through the peroxidase-like activity change-induced ionic current signatures. This study provides a new and universal strategy for distinguishing disulfide- and thiol-containing chiral molecules.

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“…In a further research, we assembled a His-rich pentapeptide (NH 2 -HHHHH-COOH) into amyloid-like structures by conjugating the oligohistidine segment to a fibril-forming peptide (NH 2 -QQKFQFQFEQQ-CONH 2 ). 72 The amyloid-like structures possessed one order higher catalytic efficiency than the oligohistidine assembly. The kinetic parameters of the peroxidase mimics are listed in Table 3 .…”

Section: Design Principle Of the Peptide-based Supramolecular Catalystsmentioning

confidence: 99%

Supramolecular enzyme-mimicking catalysts self-assembled from peptides

2023

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Self-assembly of fibril-forming histidine-rich peptides for cofactor-free oxidase-mimetic catalysis

Cited by 15 publications

References 27 publications

Enzyme-Mimicking Materials from Designed Self-Assembly of Lysine-Rich Peptides and G-Quadruplex DNA/Hemin DNAzyme: Charge Effect of the Key Residues on the Catalytic Functions

Enzyme-Mimicking Materials from Designed Self-Assembly of Lysine-Rich Peptides and G-Quadruplex DNA/Hemin DNAzyme: Charge Effect of the Key Residues on the Catalytic Functions

Target Recognition-Triggered Peroxidase-Mimicking Activity Depression in Homochiral Nanochannels for Identifying Cystine Enantiomers

Supramolecular enzyme-mimicking catalysts self-assembled from peptides

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