Tapping mode AFM study on the surface dynamics of a single glucose oxidase molecule on a Au(111) surface in water with implication for a surface-induced unfolding pathway

Otsuka, Ichiro; Yaoita, Masashi; Higano, Michi; Nagashima, Seiichi; Kataoka, Ryoichi

doi:10.1016/j.apsusc.2004.05.295

Cited by 11 publications

(8 citation statements)

References 40 publications

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“…The thicknesses of the avidin/biotin-LOD bilayer (∼3.2 nm) and avidin/biotin-LOD/avidin/biotin-HRP quadruple layer (∼5.2 nm) were smaller than the combined thickness of the closely packed protein layers using the molecular dimensions of HRP and avidin ( ca . 8−10 nm). , This is not unusual and similar results have been reported elsewhere. − ,, Since the samples for AFM measurements were rinsed with distilled water to remove salt and then dried by N 2 gas, the assembled proteins might have been partially unfolded and denatured, thus causing the decrease in height of protein layers . The AFM topographic images show that the 3D enzyme structures are well-controlled on the functional pattern region through LBL assembly.…”

Section: Resultssupporting

confidence: 82%

Controlled Assembly for Well-Defined 3D Bioarchitecture Using Two Active Enzymes

et al. 2010

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This paper reports that a bioarchitecture with two different active enzymes can be fabricated conveniently on a prepatterned surface by highly selective surface-templated layer-by-layer (LBL) assembly by coupling a bilayer of avidin/biotin-lactate oxidase (biotin-LOD) with a bilayer of avidin/biotin-horseradish peroxidase (biotin-HRP). The two different active enzymes can be utilized as excellent building blocks for the fabrication of well-defined 3D nanostructures with precise control of the position and height on the surface. In addition, the LBL assembled bienzyme structures are highly functional, and bioarchitectures based on LOD and HRP-mediated coupling reaction can be employed in a number of viable biosensing applications.

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Section: Resultssupporting

confidence: 82%

Controlled Assembly for Well-Defined 3D Bioarchitecture Using Two Active Enzymes

et al. 2010

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“…As an explanation, the affinity between the negatively charged GOD (pI = 4.2) and the positively charged surface (Calvo et al, 2001) is larger than the aggregation forces among GOD molecules, despite the high enzyme concentration (10 mg/mL) (Kurosawa et al, 1995) used. On the contrary, previous reports of AFM images of GOD adsorbed onto gold showed isolated a single molecule (Otsuka et al, 2004) or a cluster of several GOD molecules (Losic et al, 2001;Quinto et al, 1998;Zhang and Tam, 2001).…”

Section: Measurementsmentioning

confidence: 78%

Structure and biosensor characteristics of complex between glucose oxidase and plasma-polymerized nanothin film

Muguruma

Kase

2006

Biosensors and Bioelectronics

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“…Previous in situ time-lapse AFM studies have revealed height changes and lateral spreading of fibrinogen molecules adsorbed onto mica and HOPG surfaces. 15,19,30 Significant structural rearrangements of the molecule conformation, however, have not been detected. An AFM investigation of surface-induced fibrinogen unfolding in real time still remains a challenging task, possibly due to the complexity of finding an appropriate substrate surface (e.g., which would induce protein unfolding at a timescale resolvable by AFM) and physicochemical conditions favoring such a study.…”

Section: ■ Introductionmentioning

confidence: 98%

In Situ Single-Molecule AFM Investigation of Surface-Induced Fibrinogen Unfolding on Graphite

et al. 2019

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Fibrinogen adsorption plays a key role in important biological processes, such as blood coagulation and foreign body reaction, which determine the biocompatibility of a material. Fibrinogen conformation on a surface is one of the main factors triggering these processes. Understanding the conformational dynamics of fibrinogen molecules adsorbed on solid surfaces is, therefore, of great interest in biomedicine and may contribute to the development of new biomaterials. In this work, unfolding of fibrinogen molecules adsorbed on a model surface (highly oriented pyrolytic graphite modified with an oligoglycine-hydrocarbon graphite modifier) is directly visualized using time-lapse atomic force microscopy. A gradual transformation of native-like fibrinogen molecules into fibrillar structures is observed at a timescale of several minutes. This transformation is accompanied by a decrease in molecular height from 4–5 to 1–2 nm. Independent unfolding of different fibrinogen domains is demonstrated. The obtained results provide a new, direct insight into the unfolding of individual fibrinogen molecules on a surface and give new opportunities for the development of graphite-based biosensors and biomaterials.

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Tapping mode AFM study on the surface dynamics of a single glucose oxidase molecule on a Au(111) surface in water with implication for a surface-induced unfolding pathway

Cited by 11 publications

References 40 publications

Controlled Assembly for Well-Defined 3D Bioarchitecture Using Two Active Enzymes

Controlled Assembly for Well-Defined 3D Bioarchitecture Using Two Active Enzymes

Structure and biosensor characteristics of complex between glucose oxidase and plasma-polymerized nanothin film

In Situ Single-Molecule AFM Investigation of Surface-Induced Fibrinogen Unfolding on Graphite

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