Peptide-induced super-assembly of biocatalytic metal–organic frameworks for programmed enzyme cascades

Liang, Jieying; Mazur, Federico; Tang, Chuyang Y.; Ning, Xun‐an; Chandrawati, Rona; Liang, Kang

doi:10.1039/c9sc02021g

Cited by 104 publications

(92 citation statements)

References 53 publications

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“…It has been demonstrated that both of the GOx and Cyt C were uniformly embedded within the ZIF‐8 exoskeleton (Figure C and D). Previous studies have proven that small molecules, or even molecules slightly larger than the window size of ZIF‐8, are able to permeate into ZIF‐8 crystals due to the inherited flexibility of ZIF‐8 and larger defects induced by enzyme loading . Here, N 2 adsorption experiments demonstrated that the pores of the ZIF‐8 exoskeleton remained open (Figure S8A) and the unique porous structure of ZIF‐8 remained intact for both, Cyt C@ZIF‐8 and GOx@ZIF‐8 (Figure S8B).…”

Section: Resultsmentioning

confidence: 70%

Modulating the Biofunctionality of Metal–Organic‐Framework‐Encapsulated Enzymes through Controllable Embedding Patterns

et al. 2020

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Embedding an enzyme within a MOF as exoskeleton (enzyme@MOF) offers new opportunities to improve the inherent fragile nature of the enzyme, but also to impart novel biofunctionality to the MOF. Despite the remarkable stability achieved for MOF‐embedded enzymes, embedding patterns and conversion of the enzymatic biofunctionality after entrapment by a MOF have only received limited attention. Herein, we reveal how embedding patterns affect the bioactivity of an enzyme encapsulated in ZIF‐8. The enzyme@MOF can maintain high activity when the encapsulation process is driven by rapid enzyme‐triggered nucleation of ZIF‐8. When the encapsulation is driven by slow coprecipitation and the enzymes are not involved in the nucleation of ZIF‐8, enzyme@MOF tends to be inactive owing to unfolding and competing coordination caused by the ligand, 2‐methyl imidazole. These two embedding patterns can easily be controlled by chemical modification of the amino acids of the enzymes, modulating their biofunctionality.

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Section: Resultsmentioning

confidence: 70%

Modulating the Biofunctionality of Metal–Organic‐Framework‐Encapsulated Enzymes through Controllable Embedding Patterns

et al. 2020

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“…Previous studies have proven that small molecules,oreven molecules slightly larger than the window size of ZIF-8, are able to permeate into ZIF-8 crystals due to the inherited flexibility of ZIF-8 and larger defects induced by enzyme loading. [16,32,33] Here,N 2 adsorption experiments demonstrated that the pores of the ZIF-8 exoskeleton remained open ( Figure S8A) and the unique porous structure of ZIF-8 remained intact for both, Cyt C@ZIF-8 and GOx@-ZIF-8 ( Figure S8B). Them olecular size of H 2 O 2 as guest molecule for Cyt C@ZIF-8 (low activity) is smaller than that of glucose,t he guest molecule for GOx@ZIF-8 (higher activity).…”

Section: Denaturation Of Enzymes In the De Novo Embedding Strategymentioning

confidence: 99%

Modulating the Biofunctionality of Metal–Organic‐Framework‐Encapsulated Enzymes through Controllable Embedding Patterns

et al. 2020

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Embedding an enzyme within aMOF as exoskeleton (enzyme@MOF) offers new opportunities to improve the inherent fragile nature of the enzyme,but also to impart novel biofunctionality to the MOF.D espite the remarkable stability achieved for MOF-embedded enzymes,e mbedding patterns and conversion of the enzymatic biofunctionality after entrapment by aM OF have only received limited attention. Herein, we reveal howe mbedding patterns affect the bioactivity of an enzyme encapsulated in ZIF-8. The enzyme@MOF can maintain high activity when the encapsulation process is driven by rapid enzyme-triggered nucleation of ZIF-8. When the encapsulation is driven by slow coprecipitation and the enzymes are not involved in the nucleation of ZIF-8, enzy-me@MOF tends to be inactive owing to unfolding and competing coordination caused by the ligand, 2-methyl imidazole.T hese two embedding patterns can easily be controlled by chemical modification of the amino acids of the enzymes,modulating their biofunctionality.Supportinginformation and the ORCID identification number(s) for the author(s) of this article can be found under: https://doi.

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Section: Compartmentalizationmentioning

confidence: 99%

“…Very recently, our group developed a smart and stimulus-responsive approach to position discrete biocatalytic MOF nanoparticles via complementary peptide interaction (Figure 5c, i). [41] GOx, HRP or β-Gal were first separately encapsulated in ZIF-8 particles via one-step biomineralization method. Utilizing a post-ligand exchange approach, amine groups were then functionalized on the single-enzyme-containing ZIF-8.…”

Section: P E R S O N a L A C C O U N T T H E C H E M I C A L R E C O R Dmentioning

confidence: 99%

“…[39,49,50] In addition, to endow multi-enzyme catalysis with the smart and stimuli-responsive property, compartmentalization of enzymes sometimes is required to provide a separated space for different enzymes, which is helpful to regulate enzymes and enhance their whole catalytic performance. [41,55,56] More excitingly, with the merits of compartmentalization strategy and communication capability of MOFs, some chemically incompatible enzymes (e. g. protease and glucose oxidase) can be coupled together to function cooperatively for chemical synthesis. [40] Therefore, appropriate multi-enzyme immobilization strategies need to be cautiously designed.…”

Section: Introductionmentioning

confidence: 99%

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Multi‐enzyme Cascade Reactions in Metal‐organic Frameworks

Liang

2020

The Chemical Record

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Multi-enzyme cascade reactions are indispensable in biotechnology and many industrial (bio)chemical processes. However, most natural enzymes have poor stability and reusability, and tend to inactivate in toxic media or high temperature, which significantly limit their broader applications. Metal-organic frameworks (MOFs) are promising candidates for enzymes immobilization to produce nanocomposite structures that not only could shield the enzymes from harsh environments, but also facilitate selective diffusion of substrates and intermediates to the reactive site via their tailorable and ordered pore network. Multi-enzyme cascade reactions in MOFs have recently attracted considerable attention. This Personal Account discusses the different strategies for multi-enzyme-MOF interfaces and their cutting-edge applications from biosensing and catalytic nanomedicine to artificial/hybrid cells. At last, we provide a critical evaluation and future prospects to outline future research directions.

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Peptide-induced super-assembly of biocatalytic metal–organic frameworks for programmed enzyme cascades

Abstract: Complementary peptide-induced super-assembly of biocatalytic MOFs is developed for programmed enzyme cascades on demand.

Cited by 104 publications

References 53 publications

Modulating the Biofunctionality of Metal–Organic‐Framework‐Encapsulated Enzymes through Controllable Embedding Patterns

Modulating the Biofunctionality of Metal–Organic‐Framework‐Encapsulated Enzymes through Controllable Embedding Patterns

Modulating the Biofunctionality of Metal–Organic‐Framework‐Encapsulated Enzymes through Controllable Embedding Patterns

Multi‐enzyme Cascade Reactions in Metal‐organic Frameworks

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