Perspective on chymotrypsin detection

Shi, Hailong; Liu, Cheng; Cui, Jingjie; Jia, Chenglong; Lin, Yuanwei; Gao, Li; Luo, Rong

doi:10.1039/d0nj04454g

Cited by 6 publications

(3 citation statements)

References 105 publications

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“…Gold nanoparticles seem to be good alternative component for colorimetric detection or for amplification of existing signal (for example increase of Raman signal from a sample using gold nanoparticles). It is clear that efforts furthering the development of new low-cost methods, easily implementable in practice, which would be sensitive, and exhibiting long-term stability, still need to be developed [32].…”

Section: Discussionmentioning

confidence: 99%

Detection of Chymotrypsin by Optical and Acoustic Methods

2021

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Chymotrypsin is an important proteolytic enzyme in the human digestive system that cleaves milk proteins through the hydrolysis reaction, making it an interesting subject to study the activity of milk proteases. In this work, we compared detection of chymotrypsin by spectrophotometric dynamic light scattering (DLS) and quartz crystal microbalance (QCM) methods and determined the limit of chymotrypsin detection (LOD), 0.15 ± 0.01 nM for spectrophotometric, 0.67 ± 0.05 nM for DLS and 1.40 ± 0.30 nM for QCM methods, respectively. The sensors are relatively cheap and are able to detect chymotrypsin in 3035 min. While the optical detection methods are simple to implement, the QCM method is more robust for sample preparation, and allows detection of chymotrypsin in non-transparent samples. We give an overview on methods and instruments for detection of chymotrypsin and other milk proteases.

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Section: Discussionmentioning

confidence: 99%

Detection of Chymotrypsin by Optical and Acoustic Methods

2021

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“…Chymotrypsin (EC 3.4.21.1), an extensively known proteolytic enzyme that belongs to the S1 serine protease family, plays a substantial role in maintaining physiological functions including protein digestion, immune response, and tissue repair. − Meanwhile, its abnormally regulated activity is highly relevant to diseases such as pancreatitis, , diabetes, hyperinsulinemia, and pancreas carcinoma . Thus, given the significance of chymotrypsin in clinical diagnosis and drug discovery, the invention of efficient and sensitive chemical tools for its activity measurement has attracted intense attention in recent years. − Among them, a unique chymotrypsin probe design strategy was recently proposed with low cost and high atom-economy feature, which favors high-throughput screening . Different from conventional peptide-based protease-targeted probes, this “nonpeptide”-based probe design utilized the esterase activity of chymotrypsin. , Meanwhile, it has been proved to be effective in numerous following studies. − However, the ester-bond-based nature of these probes makes them possibly vulnerable to esterases, which are abundantly expressed in human fluids, and active chemicals such as hydrazine, , which are widely distributed in a polluted environment.…”

Section: Introductionmentioning

confidence: 99%

De Novo Design of a Highly Selective Nonpeptide Fluorogenic Probe for Chymotrypsin Activity Sensing in a Living System

et al. 2022

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Chymotrypsin, an extensively known proteolytic enzyme, plays a substantial role in maintaining physiological functions, including protein digestion, immune response, and tissue repair. To date, intense attention has been focused on the invention of efficient and sensitive chemical tools for chymotrypsin activity measurement. Among them, the “nonpeptide”-based chymotrypsin probe design strategy utilizing the esterase activity of chymotrypsin has been well-developed due to its low cost and high atom-economy feature. However, the ester-bond-based nature of these probes make them possibly vulnerable to esterases and active chemicals. These defects strictly restricted the application of the previously reported probes, especially for imaging in living systems. Therefore, to acquire fluorogenic probes with sufficient stability and specificity for chymotrypsin sensing in a complicated biological environment, a more stable skeleton for nonpeptide-based chymotrypsin probe construction is urgently needed. Herein, a novel nonpeptide-based fluorogenic probe for specific chymotrypsin activity sensing was designed and synthesized by the substitution of an ester-based linker with a heptafluorobutylamide moiety. The acquired probe, named TMBIHF, showed high selectivity toward various enzymes and reactive chemicals, while it retained high sensitivity and catalytic efficiency toward chymotrypsin. Moreover, TMBIHF was successfully applied for monitoring chymotrypsin activity and pancreas development in live zebrafish, specific sensing of exogenous and endogenous chymotrypsin in nude mice, and visualizing chymotrypsin-like activity-dependent cellular apoptosis, thus providing an alternative and reliable way for chymotrypsin-targeted biosensor or prodrug construction.

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“…Chymotrypsin participates in the pathogenesis of various diseases, such as diabetes, pancreatic fibrosis, hypertension, indigestion, inflammation and many cancers (particularly pancreatic cancer). [1][2][3] Therefore, developing a reliable and sensitive detection method for chymotrypsin is very important for testing pancreatic function. 4 Traditional methods such as liquid crystals (0.1 ng mL À1 ), 5 mass spectroscopy (MS, 30 pM), 6,7 quartz crystal microbalance (QCM, 1.40 nM), 8 and surface-enhanced Raman scattering (SERS, 0.4 nM) 9 are sensitive and accurate and can be used to evaluate the function of the exocrine pancreas.…”

Section: Introductionmentioning

confidence: 99%