Polydopamine functionalized nanoporous graphene foam as nanoreactor for efficient electrode-driven metabolism of steroid hormones

Xu, Xuan; Zheng, Qiqin; Bai, Guangmin; Dai, Qumei; Cao, Xiaodong; Yao, Yue; Liu, Songqin; Yang, Cheng

doi:10.1016/j.bios.2018.08.009

Cited by 20 publications

(10 citation statements)

References 61 publications

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“…To that end, P450-1A2 in complex with its redox partners (i.e., P450 reductase and cytochrome b 5 ) was adsorbed on graphite screen-printed electrodes (SPEs) coated with MWCNTs and used for quantification of the anti-inflammatory drug naproxen [181]. A similar P450-3A4/P450 reductase complex was adsorbed on 3D-nanoporous graphene foams (NCFs) and employed in detection of testosterone, estrone, and progesterone [182]. The highest activity and thermal stability of the device was achieved when the dimensions of the foam pore matched the size of the enzyme.…”

Section: Rh + O 2 + Nad(p)h + H + → Roh + H 2 O + Nad(p) + (11)mentioning

confidence: 99%

Electrocatalysis by Heme Enzymes—Applications in Biosensing

et al. 2021

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Heme proteins take part in a number of fundamental biological processes, including oxygen transport and storage, electron transfer, catalysis and signal transduction. The redox chemistry of the heme iron and the biochemical diversity of heme proteins have led to the development of a plethora of biotechnological applications. This work focuses on biosensing devices based on heme proteins, in which they are electronically coupled to an electrode and their activity is determined through the measurement of catalytic currents in the presence of substrate, i.e., the target analyte of the biosensor. After an overview of the main concepts of amperometric biosensors, we address transduction schemes, protein immobilization strategies, and the performance of devices that explore reactions of heme biocatalysts, including peroxidase, cytochrome P450, catalase, nitrite reductase, cytochrome c oxidase, cytochrome c and derived microperoxidases, hemoglobin, and myoglobin. We further discuss how structural information about immobilized heme proteins can lead to rational design of biosensing devices, ensuring insights into their efficiency and long-term stability.

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Section: Rh + O 2 + Nad(p)h + H + → Roh + H 2 O + Nad(p) + (11)mentioning

confidence: 99%

Electrocatalysis by Heme Enzymes—Applications in Biosensing

et al. 2021

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“…In the following work, Xu et al . immobilized CYP3A4 inside the nanoporous graphene foams (PNGFs) by using polydopamine as crosslinking agent to produce an efficient electrode‐driven bioreactor [101] . The optimal pore size was closed to the enzyme size implying the confinement effect on the enzyme's activity.…”

Section: Hybridization Of P450s and Materialsmentioning

confidence: 99%

“…[100] In the following work, Xu et al immobilized CYP3A4 inside the nanoporous graphene foams (PNGFs) by using polydopamine as crosslinking agent to produce an efficient electrode-driven bioreactor. [101] The optimal pore size was closed to the enzyme size implying the confinement effect on the enzyme's activity. In this work, the PNGFs not only served as the electron transfer medium between electrode and CYP3A4, but also acted as host and provided benign microenvironment for CYP-catalyzed metabolic reaction due to the unique properties of polydopamine.…”

Section: Immobilization For Electrochemical Driven Catalysismentioning

confidence: 99%

Harnessing P450 Enzyme for Biotechnology and Synthetic Biology

Zhang

Wang

2021

ChemBioChem

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Cytochrome P450 enzymes (P450s, CYPs) catalyze the oxidative transformation of a wide range of organic substrates. Their functions are crucial to xenobiotic metabolism and steroid transformation in humans and other organisms. The enzymes are promising for synthetic biology applications but limited by several drawbacks including low turnover rates, poor stability, the dependance of expensive cofactors and redox partners, and the narrow substrate scope. To conquer these obstacles, emerging strategies including substrate engineering, usage of decoy and decoy‐based small molecules auxiliaries, designing of artificial enzyme cascades and the incorporation of materials have been explored based on the unique properties of P450s. These strategies can be applied to a wide range of P450s and can be combined with protein engineering to improve the enzymatic activities. This minireview will focus on some recent developments of these strategies which have been used to leverage P450 catalysis. Remaining challenges and future opportunities will also be discussed.

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“…The biocompatible polymer polydopamine (PDA) mimics mussel byssus: it adheres firmly to almost all surfaces upon self-polymerization of dopamine in alkaline buffer. PDA offers unique properties such as cross-linking ability, excellent environmental stability, and dispersibility in water. , Inspired by the properties of PDA and its inherent reactivity toward amines, Xu et al reported the direct covalent attachment of P450-containing HLM on polydopamine-encapsulated AuNP-modified reduced graphene oxide (PDA/Au@RGO) for rapid assays of testosterone, estrone and progesterone metabolism . PDA increased sensitivity (in μA M –1 ) 2.3-fold, with K M app (testosterone) in the same range (1.6-fold lower) and twice the half-life of HLM adsorbed onto MWCNTs coated on pyrolytic graphite electrodes .…”

Section: Immobilization Of P450s By Covalent Methodsmentioning

confidence: 99%

An Overview of Cytochrome P450 Immobilization Strategies for Drug Metabolism Studies, Biosensing, and Biocatalytic Applications: Challenges and Opportunities

2021

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Cytochrome P450s (P450s or CYPs) are a large superfamily of ubiquitous heme proteins. Consistent with their natural roles in oxidative metabolism of a broad range of substrates including antibiotics and xenobiotics and in the biosynthesis of complex natural products, there are two main biotechnological applications: drug metabolism studies and biocatalytic transformations. Metabolic analyses are typically performed with the P450 enzyme immobilized on a biosensing platform. Biocatalytic reactions also increasingly make use of immobilization methods with the goal of improving operational stability of the P450s. In this Review, we briefly introduce the growing field of enzyme immobilization then focus on the advances, benefits, and challenges that apply specifically to P450s. Classical immobilization methods are presented, and recently developed materials and strategies that address the need for operational stability, the multicomponent structure of P450s, their requirement for a source of electrons, and the need to overcome limited O 2 availability are discussed in the context of metabolic, biosensing, and biocatalytic applications.

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Polydopamine functionalized nanoporous graphene foam as nanoreactor for efficient electrode-driven metabolism of steroid hormones

Cited by 20 publications

References 61 publications

Electrocatalysis by Heme Enzymes—Applications in Biosensing

Electrocatalysis by Heme Enzymes—Applications in Biosensing

Harnessing P450 Enzyme for Biotechnology and Synthetic Biology

An Overview of Cytochrome P450 Immobilization Strategies for Drug Metabolism Studies, Biosensing, and Biocatalytic Applications: Challenges and Opportunities

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