Spacer-enhanced chymotrypsin-activated peptide-functionalized gold nanoparticle probes: a rapid assay for the diagnosis of pancreatitis

Yeh, F. S.; Tseng, I-Hua; Chuang, Shu‐Hung; Lin, Chih‐Sheng

doi:10.1039/c4ra00258j

Cited by 10 publications

(16 citation statements)

References 42 publications

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“…The detection sensitivity is comparable to those of a label-free fluorometric detection of chymotrypsin activity using AuNPs, graphene oxide/DNA-stabilized silver nanoclusters, and 1,8-naphthalimide-based ratiometric fluorescence probe. 7,31,32 …”

Section: Discussionmentioning

confidence: 99%

“… 6–8 Length and charge of the peptide were considered based on the negatively charged surface of the citrate-capped AuNPs. 7,33 It is well known that conjugating with adequate ligands can improve the stability of AuNPs, and the stabilizing effect can be increased with the increase in length of the peptide. However, longer peptides may be broken easily, causing increased background for detection.…”

Section: Discussionmentioning

confidence: 99%

“…Owing to their unique physical attribute of conjugating with small molecules, we established an AuNPs-based fluorescence biosensor platform, which modified the FITC-labeled peptide onto AuNPs as the proteinase substrate. 7 Due to the quenching effect of AuNPs, once the enzyme catalyzes the substrate, the labeled FITC drifts away from the AuNPs surface, thus recovering the fluorescence signal (ESI Fig. S1 † ).…”

Section: Introductionmentioning

confidence: 99%

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Detection of chymase activity using a specific peptide probe conjugated onto gold nanoparticles

et al. 2018

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Gold nanoparticles (AuNPs) can be applied in biosensors using fluorescence resonance energy transfer (FRET) technique. Based on this technique, we have established a sensitive and efficient biosensing method by modifying a peptide-probe onto AuNPs to detect proteinase enzyme activity in this study.This biosensing method was designed for chymase activity detection and applied in kidney disease diagnosis. In this study, 16 nm-AuNPs were used to construct the AuNPs-based fluorescence peptide probe (named AuNPs-peptide probe) for chymase activity determination. The peptide sequence is FITC-Acp-DRVYIHPFHLDDDDDC, which comprises a fluorophore at the N-terminal end, an enzyme (chymase) substrate (DRVYIHPFHL), a spacer (DDDDD) and cysteine (C) to conjugate to AuNPs surface. When the enzyme catalyzes the substrate sequence, the fluorophore drifts away from AuNPs and the fluorescence emitting signal can be excited at 495 nm and detected at 515 nm. The results indicate that the time required for the AuNPs-peptide probe for activity detection of chymase was only 15 min, and a linear correlation from 10 to 100 ng mL À1 of chymase was acquired. The chymase reaction would be significantly inhibited by addition of specific chymase inhibitor chymostatin. The AuNPs-peptide probe was tested for the detection of high concentrations of trypsin and chymotrypsin, but only minor emitted fluorescence intensity was detected. According to these results, sensitivity and specificity of the AuNPspeptide probe for chymase detection have been confirmed. AuNPs-peptide probe was successfully used for the detection of renal chymase activity; and the results indicate the pathogenically increased chymase activity in kidney tissue of nephropathic mice from aristolochic acid I treatment.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Detection of chymase activity using a specific peptide probe conjugated onto gold nanoparticles

et al. 2018

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“…Chymase activity was detected using the gold nanoparticles (AuNPs)-peptide probe developed by our laboratory (FITC-Acp-DRVYIHPFHLDDDDDC-AuNPs) [27,28]. A total volume 250 μL, including AuNPs-peptide probe (125 μL), reactive buffer (pH 8, TTC buffer) and kidney tissue homogenous extract, was incubated in a micro-quartz cuvette at 37°C for 15 min.…”

Section: Methodsmentioning

confidence: 99%

Renal chymase-dependent pathway for angiotensin II formation mediated acute kidney injury in a mouse model of aristolochic acid I-induced acute nephropathy

Hsieh

Chang

et al. 2019

PLoS ONE

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Angiotensin-converting enzyme (ACE) is the primary enzyme that converts angiotensin I (Ang I) to angiotensin II (Ang II) in the renin-angiotensin system (RAS). However, chymase hydrates Ang I to Ang II independently of ACE in some kidney diseases, and it may play an important role. The present study investigated whether chymase played a crucial role in aristolochic acid I (AAI)-induced nephropathy. C57BL/6 mice were treated with AAI via intraperitoneal injection for an accumulated AAI dosage of 45 mg/kg body weight (BW) (15 mg/kg BW per day for 3 days). The animals were sacrificed after acute kidney injury development, and blood, urine and kidneys were harvested for biochemical and molecular assays. Mice exhibited increased serum creatinine, BUN and urinary protein after the AAI challenge. Significant infiltrating inflammatory cells and tubular atrophy were observed in the kidneys, and high immunocytokine levels were detected. Renal RAS-related enzyme activities were measured, and a significantly increased chymase activity and slightly decreased ACE activity were observed in the AAI-treated mice. The renal Ang II level reflected the altered profile of RAS enzymes and was significantly increased in AAI-treated mice. Treatment of AAI-induced nephropathic mice with an ACE inhibitor (ACEI) or chymase inhibitor (CI; chymostatin) reduced renal Ang II levels. The combination of ACEI and CI (ACEI+CI) treatment significantly reversed the AAI-induced changes of Ang II levels and kidney inflammation and injuries. AAI treatment significantly increased renal p-MEK without increasing p-STAT3 and p-Smad3 levels, and p-MEK/p-ERK1/2 signalling pathway was significantly activated. CI and ACEI+CI treatments reduced this AAI-activated signaling pathway. AAI-induced nephropathy progression was significantly mitigated with CI and ACEI+CI treatment. This study elucidates the role of RAS in the pathogenesis of AAI-induced nephropathy.

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“…[3][4][5][6][7][8][9][10] The appealing feature of high extinction coefficients in the visible region enables them to function as efficient quenchers for most uorophores in the design of biological sensors such as proteases, DNA and so on. [11][12][13][14][15][16] Apoptosis is an important physiological mechanism to maintain homeostasis of multicellular organisms by elimination of infected or damaged cells and regulation of cell numbers. 17,18 Caspases, which were discovered recently, are a group of cysteine proteases existing in cytoplasmic sol.…”

Section: Introductionmentioning

confidence: 99%

Coumarin-modified gold nanoprobes for the sensitive detection of caspase-3

Wang

Feng

et al. 2015

RSC Adv.

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Spacer-enhanced chymotrypsin-activated peptide-functionalized gold nanoparticle probes: a rapid assay for the diagnosis of pancreatitis

Abstract: A spacer-enhanced FITC-labeled peptide self-assembled onto AuNPs was fabricated as a chymotrypsin activated fluorescent AuNP probe and was used for the diagnosis of pancreatitis with fecal specimens.

Cited by 10 publications

References 42 publications

Detection of chymase activity using a specific peptide probe conjugated onto gold nanoparticles

Detection of chymase activity using a specific peptide probe conjugated onto gold nanoparticles

Renal chymase-dependent pathway for angiotensin II formation mediated acute kidney injury in a mouse model of aristolochic acid I-induced acute nephropathy

Coumarin-modified gold nanoprobes for the sensitive detection of caspase-3

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