An intercompartmental enzymatic cascade reaction in channel-equipped polymersome-in-polymersome architectures

Siti, Winna; Hoog, Hans‐Peter M. de; Fischer, Ozana; Shan, Wong Yee; Tomczak, Nikodem; Nallani, Madhavan; Liedberg, Bo

doi:10.1039/c3tb21849j

Cited by 52 publications

(67 citation statements)

References 43 publications

(54 reference statements)

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“…3 Enlightened by the natural cellular metabolism, a series of multienzyme conjugates were developed, and signicant enhancements in the cascade reaction kinetics and efficiency both in vivo and in vitro have been reported. [4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21] Despite the massive interests, the assembly of "in vivo" multienzyme architecture and its full understanding are always difficult due to the extreme complexity of the intracellular environment. [6][7][8] A fascinating alternative to the complex in vivo architecture is to biomimetically construct an immobilized multienzyme system that would enable efficient cascade biotransformations "in vitro".…”

Section: Introductionmentioning

confidence: 99%

Magnetic metal–organic frameworks as scaffolds for spatial co-location and positional assembly of multi-enzyme systems enabling enhanced cascade biocatalysis

et al. 2017

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Magnetic multi-enzyme nanosystems have been prepared via co-precipitation of enzymes and metalorganic framework HKUST-1 precursors in the presence of magnetic Fe 3 O 4 nanoparticles. The spatial co-localization of two enzymes was achieved using a layer-by-layer positional assembly strategy.Glucose oxidase (GOx) and horseradish peroxidase (HRP) were used as the model enzymes for cascade biocatalysis. By controlling the spatial positions of enzymes, three bienzyme nanosystems GOx@HRP@HKUST-1@Fe 3 O 4 , GOx-HRP@HKUST-1@Fe 3 O 4 and HRP@GOx@HKUST-1@Fe 3 O 4 were prepared in which GOx and HRP containing layers were in close proximity, either encapsulated in the HKUST-1 inner layer, or immobilized on the HKUST-1 outer shell, or randomly distributed in the two MOF layers. Their properties were characterized by transmission electron microscopy, energydispersive X-ray spectroscopy, Fourier transform infrared spectroscopy, X-ray diffraction, thermal gravimetric analysis, and zeta potential measurements. The highest activity was observed at pH ¼ 6 and a temperature of 20 C. Thanks to the favorable positioning of enzymes, the GOx@HRP@HKUST-

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Section: Introductionmentioning

confidence: 99%

Magnetic metal–organic frameworks as scaffolds for spatial co-location and positional assembly of multi-enzyme systems enabling enhanced cascade biocatalysis

et al. 2017

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“…Most efforts have focussed on polymersomes [17][18][19] , which lack the biological relevance of lipids, and have a diminished ability for functionalization with biological components (protein pores, receptors, antibodies and so on). They also do not possess the rich phase behaviour that lipids do, which can be taken advantage for the introduction of responsiveness.…”

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confidence: 99%

Vesicle-based artificial cells as chemical microreactors with spatially segregated reaction pathways

2014

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In the discipline of bottom-up synthetic biology, vesicles define the boundaries of artificial cells and are increasingly being used as biochemical microreactors operating in physiological environments. As the field matures, there is a need to compartmentalize processes in different spatial localities within vesicles, and for these processes to interact with one another. Here we address this by designing and constructing multi-compartment vesicles within which an engineered multi-step enzymatic pathway is carried out. The individual steps are isolated in distinct compartments, and their products traverse into adjacent compartments with the aid of transmembrane protein pores, initiating subsequent steps. Thus, an engineered signalling cascade is recreated in an artificial cellular system. Importantly, by allowing different steps of a chemical pathway to be separated in space, this platform bridges the gap between table-top chemistry and chemistry that is performed within vesicles.

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“…Release mechanisms of (macro)molecules from polymersomes without disassembly are also discussed which make use of change in the polymersome membrane permeability induced by light or by mechanical, physical, and chemical triggers . However, for the successful use of polymersomes in synthetic biology and in protocells, the interplay of other key characteristics is required. These are, for example, (i) a tunable membrane permeability with the steady accessibility of substrates for feeding enzymes into the nanoreactors and (ii) retaining the communication between polymeric compartments.…”

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confidence: 99%

Dynamic Docking and Undocking Processes Addressing Selectively the Outside and Inside of Polymersomes

İyisan

Siedel

Gumz

et al. 2017

Macromol. Rapid Commun.

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Increasing complexity and diversity of polymersomes and their compartments is a key issue for mimicking cellular functions and protocells. Thus, new challenges arise in terms of achieving tunable membrane permeability and combining it with control over the membrane diffusion process, and thus enabling a localized and dynamic control of functionality and docking possibilities within or on the surface of polymeric compartments. This study reports the concept of polymersomes with pH-tunable membrane permeability for controlling sequential docking and undocking processes of small molecules and nanometer-sized protein mimics selectively on the inside and outside of the polymersome membrane as a further step toward the design of intelligent multifunctional compartments for use in synthetic biology and as protocells. Host-guest interactions between adamantane and β-cyclodextrin as well as noncovalent interactions between poly(ethylene glycol) tails and β-cyclodextrin are used to achieve selective and dynamic functionalization of the inner and outer spheres of the polymersome membrane.

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An intercompartmental enzymatic cascade reaction in channel-equipped polymersome-in-polymersome architectures

Abstract: A multicompartment cascade reaction is presented in a polymersome-in-polymersome architecture, which is regulated by insertion of a channel protein in the inner compartment's polymer membrane.

Cited by 52 publications

References 43 publications

Magnetic metal–organic frameworks as scaffolds for spatial co-location and positional assembly of multi-enzyme systems enabling enhanced cascade biocatalysis

Magnetic metal–organic frameworks as scaffolds for spatial co-location and positional assembly of multi-enzyme systems enabling enhanced cascade biocatalysis

Vesicle-based artificial cells as chemical microreactors with spatially segregated reaction pathways

Dynamic Docking and Undocking Processes Addressing Selectively the Outside and Inside of Polymersomes

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