Peptide sequence-driven direct electron transfer properties and binding behaviors of gold-binding peptide-fused glucose dehydrogenase on electrode

Lee, Hyeryeong; Lee, Eun Mi; Reginald, Stacy Simai; Chang, In Seop

doi:10.1016/j.isci.2021.103373

Cited by 11 publications

(20 citation statements)

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“…Electrochemical K M app and I max were calculated to be 5.00 ± 0.65 mm and 118.45 ± 3.50 µA cm −2 , values in agreement with the results obtained in a previous study. [35] These results suggested that the immobilized GDHγα was highly active in glucose oxidation, implying that protein-surface interaction neither disrupted the enzyme structure nor resulted in a decreased catalysis of glucose oxidation. Based on these results taken together, it was concluded that GDHγα-3GBP could successfully construct a DET-capable enzyme-electrode system.…”

Section: Analysis Of Det Capability Wild-type and Fusion Gdhγα Protei...mentioning

confidence: 86%

“…The GDHγα-1GBP (single-repeat GBP fused to the C-terminus of the GDH α subunit) structure proven to be DETcapable on an Au electrode was initially used based on previous findings. [34,35] Then, the number of GBP repeats fused to the C-terminus of the GDH α subunit of GDHγα was modulated, producing GDHγα fusion constructs comprising a single or multiple GBP repeats. These fusion constructs were compared to each other regarding their bioactivity retention (relative to wild type) and gold-binding affinity.…”

Section: Discussionmentioning

confidence: 99%

“…In previous studies, a GBP-fused GDHγα was strategically designed to enforce a particular orientation of the enzyme cofactor relative to the electrode, specifically an orientation compatible with DET between the cofactor and the surface at the enzyme-electrode interface. [34,35] In those studies, the optimal DET rate could be obtained from the fusion of the GBP with an MHGKTQATSGTIQS sequence at the C-terminus of the GDH α subunit. Based on this information, the number of GBP repeats fused at the C-terminus of the α subunit was modulated under the assumption that the gold-recognition ability of GDHγα constructs would be proportional to the number of copies of the gold-binding motif included in the GBP portion of the construct.…”

Section: Determination Of the Ideal Number Of Tandem Gbp Repeats Fuse...mentioning

confidence: 99%

“…SBP sequence Catalytic activity ✓ Catalytic activity of enzyme tends to be highly preserved after genetic SBP fusion. [35] Inorganic-binding activity ✓ The amino acid contents and conformation of SBP determines inorganic-adsorption activities. ✓ The inorganic binding affinities (K eq ) of fusion enzymes with various GBP sequences are primarily determined by adsorption kinetics, rather than desorption kinetics.…”

Section: Design Factors Performance Parametersmentioning

confidence: 99%

“…Furthermore, to investigate the effect of GBP type on the cofactor-surface orientation, the above GBP, LKAHLPPSRLPS, and three other GBPs (MHGKTQATSGTIQS, TGTSVLIATPGV, and VSGSSPDS) were fused in four respective experiments to the same enzyme site. [35] The different types of GBP yielded significantly different cofactor-surface orientations and interfacial ET rates, attributed to the different GBPs having different conformations related to their different sequences and lengths.…”

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confidence: 99%

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Versatile Biosynthetic Approach to Regioselective Enzyme Patterning for Direct Bioelectrocatalysis Application

Lee

Reginald

Chang

2023

Adv Materials Technologies

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accomplish enzymatic catalysis with high catalytic efficiency. [6,7] Specifically, such a spatial organization of enzymes enables the efficient delivery of metabolites among enzyme active sites while preventing the steric hindrance of a reaction site by adjacent proteins. [8] Therefore, it is essential to consider the effect of enzyme spatial organization on overall metabolic efficiency for translating our knowledge about natural biochemical systems into noncellular artificial environments, such as those involving electrodes. [9] Inspired by nature, a generation of proper multior single enzymatic positioning on electrodes can bring about enhanced performance of enzyme-based bioelectrocatalysis systems. [10] Regarding in vitro spatial organization, there have been considerable efforts to achieve technical advances in position-specific enzyme immobilization by performing "protein patterning". [11,12] Protein molecules have been patterned using direct or indirect assembly (i.e., self-assembled monolayers alkanethiol, silane, Ni-NTA, biotin, etc.) by integration with lithographic approaches including scanning probe microscopy, [13,14] dip-pen nanolithography (DPN), [15] atomic force microscopy (AFM), [16] electron beam (e-beam) lithography (EBL), [17] and nanoimprint lithography (NIL). [18] DNA templates have also been widely used to create periodic arrays of protein molecules. [19] Yan et al. (2003) reported that DNA tiles with sticky ends self-assembled into nanoribbons or nanogrids that provided a predetermined surface for target-molecule binding. [20] Since the enzyme-based electrocatalysis system operates cooperatively by single-or multienzyme-based catalysis and electron transfer (ET) between the enzymatic cofactor and electrode, electrical communication of the enzyme-electrode should also be considered and controlled together with enzymatic surface-positioning. [21,22] However, most of the previous studies involving the development of protein micro/nanopatterning techniques were not primarily concerned with the enzymeelectrode interface. The approaches for protein patterning have not proven to be amenable in controlling the orientations of enzymes on surfaces. Hence, extensive chemical/biochemical surface modification or random attachments of the protein may electrically block the cofactor-surface interfaces, limiting the interfacial efficiency of direct ET (DET). [23] Due to the outstanding attributes of oxidoreductases, they have been utilized as biomaterials for bioelectrocatalytic systems. Herein, a simple and versatile biosynthetic approach that can designate binding position of enzymes on electrode with their surface-orientation is suggested. In this regard, materialselective properties of gold-binding peptide (GBP) are exploited and genetically fused GBP to enzyme. To optimize the design of synthetic enzyme, a variable repeat number of GBP are fused to flavin adenine dinucleotidedependent glucose dehydrogenase gamma-alpha complex (GDHγα) and their catalytic and gold-binding activities are determined. T...

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Section: Analysis Of Det Capability Wild-type and Fusion Gdhγα Protei...mentioning

confidence: 86%

Section: Discussionmentioning

confidence: 99%

Section: Determination Of the Ideal Number Of Tandem Gbp Repeats Fuse...mentioning

confidence: 99%

Section: Design Factors Performance Parametersmentioning

confidence: 99%

mentioning

confidence: 99%

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