Protease Amperometric Sensor

Ionescu, Rodica Elena; Cosnier, Serge; Marks, Robert S.

doi:10.1021/ac060253w

Cited by 93 publications

(65 citation statements)

References 23 publications

(37 reference statements)

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“…12 Ionescu et al introduced an amperometric sensor coated with gelatine for the detection of trypsin. 13 Other natural protease substrates used in this sensor format included fibrinogen used for the detection of human neutrophil elastase by quartz crystal microbalance (QCM) and BSA cross-linked acrylamide degraded by pepsin. 18 All of the protease sensors mentioned above are based on the measurement of the disappearance of the film from the transducer surface.…”

Section: Protease Sensors Based On the Degradation Of Thin Filmsmentioning

confidence: 99%

Generic protease detection technology for monitoring periodontal disease

et al. 2011

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Periodontal diseases are inflammatory conditions that affect the supporting tissues of teeth and can lead to destruction of the bone support and ultimately tooth loss if untreated. Progression of periodontitis is usually site specific but not uniform, and currently there are no accurate clinical methods for distinguishing sites where there is active disease progression from sites that are quiescent. Consequently, unnecessary and costly treatment of periodontal sites that are not progressing may occur. Three proteases have been identified as suitable markers for distinguishing sites with active disease progression and quiescent sites: human neutrophil elastase, cathepsin G and MMP8. Generic sensor materials for the detection of these three proteases have been developed based on thin dextran hydrogel films cross-linked with peptides. Degradation of the hydrogel films was monitored using impedance measurements. The target proteases were detected in the clinically relevant range within a time frame of 3 min. Good specificity for different proteases was achieved by choosing appropriate peptide cross-linkers.

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Section: Protease Sensors Based On the Degradation Of Thin Filmsmentioning

confidence: 99%

Generic protease detection technology for monitoring periodontal disease

et al. 2011

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“…To solve these problems, many new methods have been reported, including colorimetry, chemiluminescence, fluorescence, and electrochemical. [11][12][13][14]25 Among them, a fluorescence method has attracted immense interest owing to its rapid response and easy operation.…”

Section: Introductionmentioning

confidence: 99%

A Label-free Fluorescence Assay for Trypsin Based on the Electron Transfer between Oligonucleotide-stabilized Ag Nanoclusters and Cytochrome c

Hong

Han

et al. 2014

ANAL. SCI.

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Herein we attempt to develop a simple, specific and costeffective fluorescent method for trypsin activity assay through the combination of Cyt c and Ag NCs. The assay principle is elaborated in Scheme 1. We firstly synthesize oligonucleotide-2014 © The Japan Society for Analytical Chemistry † To whom correspondence should be addressed. A label-free fluorescent assay for the detection of trypsin by using oligonucleotide-templated silver nanoclusters (Ag NCs) and cytochrome c (Cyt c) has been demonstrated. When negatively charged Ag NCs and positively charged Cyt c are mixed, they tend to form a hybrid complex, and then lead the fluorescence of Ag NCs to be quenched significantly due to electron transfer between Ag NCs and the heme cofactor of Cyt c. In the presence of trypsin, it catalyzes the hydrolytic cleavage of Cyt c to small peptide fragments, and releases the heme moiety from the Ag NCs/Cyt c complex; the quenched fluorescence restores therewith. By virtue of this specific response, the fluorescent biosensor has a linear range of from 0.7 to 4 μg mL -1 and from 9 to 120 μg mL -1 with a detection limit of 58.7 ng mL -1. Aside from the easy manufacture aspect, our method also possesses a high signal-to-background ratio (~11), excellent selectivity and good biocompatibility, which makes it a promising bioanalysis for a trypsin activity assay. Keywords

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“…Therefore, the determination of protease activities is of great importance from the physiological and pathological points of view. Nowadays, various chemical sensors have been prepared using proteases for cleaving peptide chains followed by appropriate signal transductions including spectrophotometry [6], colorimetry [7], fluorimetry [8], radiometry [9], holography [10], chromatography [11], amperometry [12], alternating current impedance [13], conductometry [14], and potentiometry [15]. Among these sensors, the potentiometric polyion sensor has appeared very promising for monitoring protease activities [16][17][18][19][20].…”

Section: Introductionmentioning

confidence: 99%