A Ratiometric Fluorescent Probe for Monitoring Leucine Aminopeptidase in Living Cells and Zebrafish Model

Zhou, Zhe; Wang, Feiyi; Yang, Guichun; Lu, Cuifen; Nie, Junqi; Chen, Zuxing; Ren, Jing; Sun, Qi; Zhao, Chunchang; Zhu, Weihong

doi:10.1021/acs.analchem.7b02910

Cited by 89 publications

(31 citation statements)

References 45 publications

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“…The L-Ala and L-Leu anilides of 6-aminoluciferin were used to successfully image APN in xenografted luciferase-expressing tumors in nude mice (Li et al 2014); light production was decreased by administration of the APN inhibitor bestatin (267, Figure 22). A boron-dipyrromethylene (BODIPY) core bearing a L-Cys-L-Leu moiety (BODIPY-C-Leu) is biotransformed by APN to the BODIPY-Cys intermediate that undergoes a S to N migration to give the highly fluorescent BODIPY-N-Cys (Zhou et al 2017); BODIPY-Leu successfully imaged APN in HeLa cells and in zebrafish, and light production was decreased by the APN inhibitor bestatin (267, Figure 22).…”

Section: Substrates Apn Catalyzes the Hydrolysis Of N-ter-mentioning

confidence: 99%

The mercapturic acid pathway

Hanna

Anders

2019

Critical Reviews in Toxicology

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The mercapturic acid pathway is a major route for the biotransformation of xenobiotic and endobiotic electrophilic compounds and their metabolites. Mercapturic acids (N-acetyl-L-cysteine S-conjugates) are formed by the sequential action of the glutathione transferases, c-glutamyltransferases, dipeptidases, and cysteine S-conjugate N-acetyltransferase to yield glutathione S-conjugates, L-cysteinylglycine S-conjugates, L-cysteine S-conjugates, and mercapturic acids; these metabolites constitute a "mercapturomic" profile. Aminoacylases catalyze the hydrolysis of mercapturic acids to form cysteine S-conjugates. Several renal transport systems facilitate the urinary elimination of mercapturic acids; urinary mercapturic acids may serve as biomarkers for exposure to chemicals. Although mercapturic acid formation and elimination is a detoxication reaction, L-cysteine S-conjugates may undergo bioactivation by cysteine Sconjugate b-lyase. Moreover, some L-cysteine S-conjugates, particularly L-cysteinyl-leukotrienes, exert significant pathophysiological effects. Finally, some enzymes of the mercapturic acid pathway are described as the so-called "moonlighting proteins," catalytic proteins that exert multiple biochemical or biophysical functions apart from catalysis.

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Section: Substrates Apn Catalyzes the Hydrolysis Of N-ter-mentioning

confidence: 99%

The mercapturic acid pathway

Hanna

Anders

2019

Critical Reviews in Toxicology

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“…Their additional advantage is the ease of functionalization. Owing to the above properties, difluoroboranes have been used as optical switches [26][27][28][29][30][31], fluorescent probes [32][33][34][35][36][37][38], photosensitizers used in photochemotherapy [39][40][41][42][43][44][45], biomarkers [46][47][48][49][50], and TADF (Thermally-Activated Delayed Fluorescence) materials used for emitters for organic light-emitting diodes [51][52][53][54], among others.…”

Section: Introductionmentioning

confidence: 99%

Benchmarking Density Functional Approximations for Excited-State Properties of Fluorescent Dyes

Grabarz

Ośmiałowski

2021

Molecules

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This study presents an extensive analysis of the predictive power of time-dependent density functional theory in determining the excited-state properties of two groups of important fluorescent dyes, difluoroboranes and hydroxyphenylimidazo[1,2-a]pyridine derivatives. To ensure statistically meaningful results, the data set is comprised of 85 molecules manifesting diverse photophysical properties. The vertical excitation energies and dipole moments (in the electronic ground and excited states) of the aforementioned dyes were determined using the RI-CC2 method (reference) and with 18 density functional approximations (DFA). The set encompasses DFAs with varying amounts of exact exchange energy (EEX): from 0% (e.g., SVWN, BLYP), through a medium (e.g., TPSSh, B3LYP), up to a major contribution of EEX (e.g., BMK, MN15). It also includes range-separated hybrids (CAM-B3LYP, LC-BLYP). Similar error profiles of vertical energy were obtained for both dye groups, although the errors related to hydroxyphenylimidazopiridines are significantly larger. Overall, functionals including 40–55% of EEX (SOGGA11-X, BMK, M06-2X) ensure satisfactory agreement with the reference vertical excitation energies obtained using the RI-CC2 method; however, MN15 significantly outperforms them, providing a mean absolute error of merely 0.04 eV together with a very high correlation coefficient (R2 = 0.98). Within the investigated set of functionals, there is no single functional that would equally accurately determine ground- and excited-state dipole moments of difluoroboranes and hydroxyphenylimidazopiridine derivatives. Depending on the chosen set of dyes, the most accurate μGS predictions were delivered by MN15 incorporating a major EEX contribution (difluoroboranes) and by PBE0 containing a minor EEX fraction (hydroxyphenylimidazopiridines). Reverse trends are observed for μES, i.e., for difluoroboranes the best results were obtained with functionals including a minor fraction of EEX, specifically PBE0, while in the case of hydroxyphenylimidazopiridines, much more accurate predictions were provided by functionals incorporating a major EEX contribution (BMK, MN15).

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“…LAPs are a class of metal peptidases that hydrolyze leucine residues at the amino terminus of a protein or peptide substrate 59 . LAPs are involved in various physiological processes, including hydrolysis of biologically active peptides 98 , degradation of DNA 99 , and interaction with peptide-dependent signals 100 . LAPs play a vital role in normal functioning of the body 56 .…”

Section: Peptide/group Selective To Enzymesmentioning

confidence: 99%

Activated molecular probes for enzyme recognition and detection

Yuan¹,

Wu²,

Zhao³

et al. 2022

Theranostics

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Exploring and understanding the interaction of changes in the activities of various enzymes, such as proteases, phosphatases, and oxidoreductases with tumor invasion, proliferation, and metastasis is of great significance for early cancer diagnosis. To detect the activity of tumor-related enzymes, various molecular probes have been developed with different imaging methods, including optical imaging, photoacoustic imaging (PAI), magnetic resonance imaging, positron emission tomography, and so on. In this review, we first describe the biological functions of various enzymes and the selectively recognized chemical linkers or groups. Subsequently, we systematically summarize the design mechanism of imaging probes and different imaging methods. Finally, we explore the challenges and development prospects in the field of enzyme activity detection. This comprehensive review will provide more insight into the design and development of enzyme activated molecular probes.

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A Ratiometric Fluorescent Probe for Monitoring Leucine Aminopeptidase in Living Cells and Zebrafish Model

Cited by 89 publications

References 45 publications

The mercapturic acid pathway

The mercapturic acid pathway

Benchmarking Density Functional Approximations for Excited-State Properties of Fluorescent Dyes

Activated molecular probes for enzyme recognition and detection

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