Phosphine mediated conjugation of S-nitrosothiols and aldehydes

Biggs, Tyler D.; Weerasinghe, Laksiri; Park, Chung‐Min; Xian, Ming

doi:10.1016/j.tetlet.2015.04.017

Cited by 7 publications

(6 citation statements)

References 22 publications

(14 reference statements)

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“…This intermediate is further hydrolyzed to produce the phosphoryl-disulfide product 2 (derivatized GSNO). 18,31 …”

Section: Resultsmentioning

confidence: 99%

“…This intermediate is further hydrolyzed to produce the phosphoryl-disulfide product 2 (derivatized GSNO). 18,31 The derivatized GSNO (product 2) was detected by QTOF MS in positive mode (monitored/expected masses, m/z = 616.1356/616.1341 [M + H] + ). MS/MS analysis confirmed this identification (Figure 3A).…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…Because the sulfur atom in the reagent is directly bonded to the phenyl ring, the resulting aza-ylide leads to a pseudo -sulfenamide intermediate which is then attacked by the intramolecular phenylthiolate to yield a disulfide-iminophosphorane structure 1. This intermediate is further hydrolyzed to produce the phosphoryl-disulfide product 2 (derivatized GSNO). , …”

Section: Resultsmentioning

confidence: 99%

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Automated Online Solid-Phase Derivatization for Sensitive Quantification of Endogenous S-Nitrosoglutathione and Rapid Capture of Other Low-Molecular-Mass S-Nitrosothiols

et al. 2018

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S-Nitrosothiols (RSNOs) constitute a circulating endogenous reservoir of nitric oxide, and have important biological activities. In this study, an online coupling of solid phase derivatization (SPD) with liquid chromatography-mass spectrometry (LC-MS) was developed and applied in the analysis of low-molecular-mass RSNOs. A derivatizing-reagent-modified polymer monolithic column was prepared and adapted for online SPD-LC-MS. Analytes from the LC auto-sampler flowed through the monolithic column for derivatization, and then directly into the LC-MS for analysis. This integration of the online derivatization, LC separation and MS detection facilitated system automation, allowing rapid, laborsaving, and sensitive detection of RSNOs. S-Nitrosoglutathione (GSNO) was quantified using this automated online method with good linearity (R2 = 0.9994); the limit of detection was 0.015 nM. The online SPD-LC-MS method has been used to determine GSNO levels in mouse samples, 138 ± 13.2 nM of endogenous GSNO was detected in mouse plasma. Besides, the GSNO concentrations in liver (64.8 ± 11.3 pmol/mg protein), kidney (47.2 ± 6.1 pmol/mg protein), heart (8.9 ± 1.8 pmol/mg protein), muscle (1.9 ± 0.3 pmol/mg protein), hippocampus (5.3 ± 0.9 pmol/mg protein), striatum (6.7 ± 0.6 pmol/mg protein), cerebellum (31.4 ± 6.5 pmol/mg protein), and cortex (47.9 ± 4.6 pmol/mg protein) were also successfully quantified. When the derivatization was performed within 8 minutes, followed by LC-MS detection, samples could be rapidly analyzed compared with the offline manual method. Other low-molecular-mass RSNOs, such as S-nitrosocysteine and S-nitrosocysteinylglycine, were captured by rapid precursor-ion scanning, showing that the proposed method is a potentially powerful tool for capture, identification and quantification of RSNOs in biological samples.

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“…This intermediate is further hydrolyzed to produce the phosphoryl-disulfide product 2 (derivatized GSNO). 18,31 …”

Section: Resultsmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Automated Online Solid-Phase Derivatization for Sensitive Quantification of Endogenous S-Nitrosoglutathione and Rapid Capture of Other Low-Molecular-Mass S-Nitrosothiols

et al. 2018

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“…The SNOTRAP approach is a direct labeling strategy in which triphenylphosphine thioester can specifically react with the SNO group to stabilize the disulfide–iminophosphorane product with good yields under mild conditions. − A biotin group linked to triphenylphosphine thioester allows enrichment of SNOTRAP-modified proteins on streptavidin beads (Figure ), which achieves site-specific identification of SNO–proteome. In addition, a series of triphenylphosphine derivatives has been reported to selectively react with SNO groups, including but not limited to triphenylphosphine, trialkylphosphine, triphenylphosphine esters, water-soluble phosphine, 2-(diphenylphosphanyl)-benzothioate, and 2-(diphenylphosphanyl)-benzaldehyde . These phosphine compounds have the potential for SNO detection in biological systems.…”

Section: Proteomic Approaches For Site-specific Identification and Ch...mentioning

confidence: 99%

Protein S-Nitrosation: Biochemistry, Identification, Molecular Mechanisms, and Therapeutic Applications

Liang

et al. 2022

J. Med. Chem.

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Protein S-nitrosation (SNO), a posttranslational modification (PTM) of cysteine (Cys) residues elicited by nitric oxide (NO), regulates a wide range of protein functions. As a crucial form of redox-based signaling by NO, SNO contributes significantly to the modulation of physiological functions, and SNO imbalance is closely linked to pathophysiological processes. Site-specific identification of the SNO protein is critical for understanding the underlying molecular mechanisms of protein function regulation. Although careful verification is needed, SNO modification data containing numerous functional proteins are a potential research direction for druggable target identification and drug discovery. Undoubtedly, SNO-related research is meaningful not only for the development of NO donor drugs but also for classic target-based drug design. Herein, we provide a comprehensive summary of SNO, including its origin and transport, identification, function, and potential contribution to drug discovery. Importantly, we propose new views to develop novel therapies based on potential protein SNO-sourced targets.

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“…Thus, numerous selective thiol probes have emerged in the literature. − In contrast to the ease of measurement of small molecule thiols, it possesses difficulties and challenges to concisely detect a certain type of protein thiol modifications. Nevertheless, the strong nucleophilic property of the sulfhydryl group opens a window to chemically label protein thiols with specific thiol-reactive agents and hence enables reliable and robust detection of protein thiol modifications. ,,− …”

mentioning

confidence: 99%

Naphthalimide Scaffold Provides Versatile Platform for Selective Thiol Sensing and Protein Labeling

Zhou

Yao

et al. 2016

ACS Chem. Biol.

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Reversible thiol modifications are fundamental of cellular redox regulation. Specific thiol detection, including thiol sensing and protein thiols labeling, is critical to study such modifications. We reported the discovery of 4-methylsulfonyl-N-n-butyl-1,8-naphthalimide (MSBN), a highly selective fluorogenic probe for thiols based on the 1,8-naphthalimide scaffold. Thiols react with MSBN nearly quantitatively via nucleophilic aromatic substitution to replace the methylsulfonyl group and restore the quenched fluorescence (>100-fold increase). MSBN was employed to selectively image thiols in live cells and specifically label protein thiols with a turn-on signal to determine diverse reversible protein thiol modifications. In addition, we introduced a bulky group into the MSBN as a mass tag to create a probe MSBN-TPP, which readily discriminates the reduced thioredoxin from the oxidized one. The specific reaction of MSBN with thiols and the easy manipulation of the naphthalimide unit enable MSBN a versatile scaffold in developing novel probes for thiol-based protein bioconjugation and studying various thiol modifications.

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Phosphine mediated conjugation of S-nitrosothiols and aldehydes

Cited by 7 publications

References 22 publications

Automated Online Solid-Phase Derivatization for Sensitive Quantification of Endogenous S-Nitrosoglutathione and Rapid Capture of Other Low-Molecular-Mass S-Nitrosothiols

Automated Online Solid-Phase Derivatization for Sensitive Quantification of Endogenous S-Nitrosoglutathione and Rapid Capture of Other Low-Molecular-Mass S-Nitrosothiols

Protein S-Nitrosation: Biochemistry, Identification, Molecular Mechanisms, and Therapeutic Applications

Naphthalimide Scaffold Provides Versatile Platform for Selective Thiol Sensing and Protein Labeling

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