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

Summary: Oriented enzyme immobilization on electrodes is crucial for interfacial electrical coupling of direct electron transfer (DET)-based enzyme-electrode systems. As inorganic-binding peptides are introduced as molecular binders and enzyme-orienting agents, inorganic-binding peptide-fused enzyme...

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Autores principales:	Hyeryeong Lee, Eun Mi Lee, Stacy Simai Reginald, In Seop Chang
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Electrochemistry Bio-electrochemistry Materials science Materials chemistry Science Q
Acceso en línea:	https://doaj.org/article/edec74f7998747f5872c0ee1ca85ea42
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spelling	oai:doaj.org-article:edec74f7998747f5872c0ee1ca85ea422021-11-20T05:10:49ZPeptide sequence-driven direct electron transfer properties and binding behaviors of gold-binding peptide-fused glucose dehydrogenase on electrode2589-004210.1016/j.isci.2021.103373https://doaj.org/article/edec74f7998747f5872c0ee1ca85ea422021-11-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2589004221013444https://doaj.org/toc/2589-0042Summary: Oriented enzyme immobilization on electrodes is crucial for interfacial electrical coupling of direct electron transfer (DET)-based enzyme-electrode systems. As inorganic-binding peptides are introduced as molecular binders and enzyme-orienting agents, inorganic-binding peptide-fused enzymes should be designed and constructed to achieve efficient DET. In this study, it is aimed to compare the effects of various gold-binding peptides (GBPs) fused to enzymes on electrocatalytic activity, bioactivity, and material-binding behaviors. Here, GBPs with identical gold-binding properties but different amino acid sequences were fused to the FAD-dependent glucose dehydrogenase gamma-alpha complex (GDHγα) to generate four GDHγα variants. The structural, biochemical, mechanical, and bioelectrochemical properties of these GDHγα variants immobilized on electrode were determined by their fused GBPs. Our results confirmed that the GBP type is vital in the design, construction, and optimization of GBP-fused enzyme-modified electrodes for facile interfacial DET and practical DET-based enzyme-electrode systems.Hyeryeong LeeEun Mi LeeStacy Simai ReginaldIn Seop ChangElsevierarticleElectrochemistryBio-electrochemistryMaterials scienceMaterials chemistryScienceQENiScience, Vol 24, Iss 11, Pp 103373- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Electrochemistry Bio-electrochemistry Materials science Materials chemistry Science Q
spellingShingle	Electrochemistry Bio-electrochemistry Materials science Materials chemistry Science Q Hyeryeong Lee Eun Mi Lee Stacy Simai Reginald In Seop Chang Peptide sequence-driven direct electron transfer properties and binding behaviors of gold-binding peptide-fused glucose dehydrogenase on electrode
description	Summary: Oriented enzyme immobilization on electrodes is crucial for interfacial electrical coupling of direct electron transfer (DET)-based enzyme-electrode systems. As inorganic-binding peptides are introduced as molecular binders and enzyme-orienting agents, inorganic-binding peptide-fused enzymes should be designed and constructed to achieve efficient DET. In this study, it is aimed to compare the effects of various gold-binding peptides (GBPs) fused to enzymes on electrocatalytic activity, bioactivity, and material-binding behaviors. Here, GBPs with identical gold-binding properties but different amino acid sequences were fused to the FAD-dependent glucose dehydrogenase gamma-alpha complex (GDHγα) to generate four GDHγα variants. The structural, biochemical, mechanical, and bioelectrochemical properties of these GDHγα variants immobilized on electrode were determined by their fused GBPs. Our results confirmed that the GBP type is vital in the design, construction, and optimization of GBP-fused enzyme-modified electrodes for facile interfacial DET and practical DET-based enzyme-electrode systems.
format	article
author	Hyeryeong Lee Eun Mi Lee Stacy Simai Reginald In Seop Chang
author_facet	Hyeryeong Lee Eun Mi Lee Stacy Simai Reginald In Seop Chang
author_sort	Hyeryeong Lee
title	Peptide sequence-driven direct electron transfer properties and binding behaviors of gold-binding peptide-fused glucose dehydrogenase on electrode
title_short	Peptide sequence-driven direct electron transfer properties and binding behaviors of gold-binding peptide-fused glucose dehydrogenase on electrode
title_full	Peptide sequence-driven direct electron transfer properties and binding behaviors of gold-binding peptide-fused glucose dehydrogenase on electrode
title_fullStr	Peptide sequence-driven direct electron transfer properties and binding behaviors of gold-binding peptide-fused glucose dehydrogenase on electrode
title_full_unstemmed	Peptide sequence-driven direct electron transfer properties and binding behaviors of gold-binding peptide-fused glucose dehydrogenase on electrode
title_sort	peptide sequence-driven direct electron transfer properties and binding behaviors of gold-binding peptide-fused glucose dehydrogenase on electrode
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/edec74f7998747f5872c0ee1ca85ea42
work_keys_str_mv	AT hyeryeonglee peptidesequencedrivendirectelectrontransferpropertiesandbindingbehaviorsofgoldbindingpeptidefusedglucosedehydrogenaseonelectrode AT eunmilee peptidesequencedrivendirectelectrontransferpropertiesandbindingbehaviorsofgoldbindingpeptidefusedglucosedehydrogenaseonelectrode AT stacysimaireginald peptidesequencedrivendirectelectrontransferpropertiesandbindingbehaviorsofgoldbindingpeptidefusedglucosedehydrogenaseonelectrode AT inseopchang peptidesequencedrivendirectelectrontransferpropertiesandbindingbehaviorsofgoldbindingpeptidefusedglucosedehydrogenaseonelectrode
_version_	1718419575104602112

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

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