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Bo Tang - One of the best experts on this subject based on the ideXlab platform.

  • cyclic regulation of the sulfilimine bond in peptides and nc1 hexamers via the hobr h2se conjugated system
    Analytical Chemistry, 2018
    Co-Authors: Dongrui Luan, Aishan Zheng, Fanpeng Kong, Kehua Xu, Xiaoxiao Song, Bo Tang
    Abstract:

    The sulfilimine bond (−S═N−), found in the collagen IV scaffold, significantly stabilizes the architecture via the formation of sulfilimine cross-links. However, precisely governing the formation and breakup process of the sulfilimine bond in living organisms for better life functions still remains a challenge. Hence, we established a new way to regulate the breaking and formation of the sulfilimine bond through hydrogen selenide (H2Se) and Hypobromous Acid (HOBr), which can be easily controlled at simulated physiological conditions. This novel strategy provides a circulation regulation system to modulate the sulfilimine bond in peptides and NC1 hexamers, which can offer a substantial system for further study of the physiological function of collagen IV.

  • Cyclic Regulation of the Sulfilimine Bond in Peptides and NC1 Hexamers via the HOBr/H2Se Conjugated System
    2018
    Co-Authors: Dongrui Luan, Aishan Zheng, Fanpeng Kong, Xiaoxiao Song, Xiaojun Liu, Xiaonan Gao, Bo Tang
    Abstract:

    The sulfilimine bond (−SN−), found in the collagen IV scaffold, significantly stabilizes the architecture via the formation of sulfilimine cross-links. However, precisely governing the formation and breakup process of the sulfilimine bond in living organisms for better life functions still remains a challenge. Hence, we established a new way to regulate the breaking and formation of the sulfilimine bond through hydrogen selenide (H2Se) and Hypobromous Acid (HOBr), which can be easily controlled at simulated physiological conditions. This novel strategy provides a circulation regulation system to modulate the sulfilimine bond in peptides and NC1 hexamers, which can offer a substantial system for further study of the physiological function of collagen IV

  • high quantum yield mitochondria targeting near infrared fluorescent probe for imaging native Hypobromous Acid in living cells and in vivo
    Analytical Chemistry, 2017
    Co-Authors: Xiaojun Liu, Dongrui Luan, Aishan Zheng, Fanpeng Kong, Xiaoting Wang, Lili Tong, Bo Tang
    Abstract:

    The discovery that Hypobromous Acid (HOBr) can regulate the activity of collagen IV has attracted great attention. However, HOBr as an important reactive small molecule has hardly ever been studied using a detection method suitable for organisms. Herein, a high-quantum-yield mitochondria-targeting near-infrared (NIR) fluorescent probe for HOBr, RhSN-mito, was designed. RhSN-mito was easily obtained by the Suzuki cross-coupling reaction. The test results show that RhSN-mito can rapidly respond to HOBr with ultrasensitivity and high selectivity. The achievement of ultrasensitivity lies in the high signal-to-noise ratio and the highest fluorescence quantum yield of the reaction product (ΦF = 0.68) in the near-infrared region, as far as we know. RhSN-mito is successfully applied to image native HOBr in mitochondria of HepG2 cells and zebrafish. Thus, RhSN-mito is a powerful tool for detecting native HOBr in vivo and is expected to provide a method to further study the physiological and pathological functions ...

  • High-Quantum-Yield Mitochondria-Targeting Near-Infrared Fluorescent Probe for Imaging Native Hypobromous Acid in Living Cells and in Vivo
    2017
    Co-Authors: Xiaojun Liu, Dongrui Luan, Aishan Zheng, Fanpeng Kong, Xiaoting Wang, Lili Tong, Bo Tang
    Abstract:

    The discovery that Hypobromous Acid (HOBr) can regulate the activity of collagen IV has attracted great attention. However, HOBr as an important reactive small molecule has hardly ever been studied using a detection method suitable for organisms. Herein, a high-quantum-yield mitochondria-targeting near-infrared (NIR) fluorescent probe for HOBr, RhSN-mito, was designed. RhSN-mito was easily obtained by the Suzuki cross-coupling reaction. The test results show that RhSN-mito can rapidly respond to HOBr with ultrasensitivity and high selectivity. The achievement of ultrasensitivity lies in the high signal-to-noise ratio and the highest fluorescence quantum yield of the reaction product (ΦF = 0.68) in the near-infrared region, as far as we know. RhSN-mito is successfully applied to image native HOBr in mitochondria of HepG2 cells and zebrafish. Thus, RhSN-mito is a powerful tool for detecting native HOBr in vivo and is expected to provide a method to further study the physiological and pathological functions related to HOBr

Heng Liu - One of the best experts on this subject based on the ideXlab platform.

  • a novel near infrared fluorescent probe for detection of Hypobromous Acid and its bioimaging applications
    Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 2019
    Co-Authors: Xiaoyu Zhang, Heng Liu
    Abstract:

    Abstract Hypobromous Acid (HOBr) is an important reactive oxygen species and has been recently found to be associated with a variety of diseases. However, owing to a lack of effective analytical tools, there is still limited understanding of its roles in living systems. Here, we present a new type of near-infrared fluorescent probe DCSN for HOBr detection. The designed probe exhibits high sensitivity with a low detection limit, excellent selectivity over other interfering species and low cytotoxicity. More interestingly, the fluorescence response behavior of the probe was different from the previous literatures due to the intramolecular charge transfer process. Moreover, we have successfully monitored HOBr in living cells by utilizing DCSN. This probe has potential to be used as a promising tool for better understanding the physiological functions of HOBr.

  • lysosome targetable red emitting ratiometric fluorescent probe for Hypobromous Acid imaging in living cells
    Sensors and Actuators B-chemical, 2019
    Co-Authors: Deman Han, Xinxin Zhong, Caixia Chen, Xiuxia Liang, Heng Liu
    Abstract:

    Abstract As one of the most important reactive oxygen species, Hypobromous Acid (HOBr) has been reported to be linked to a large body of diseases. Although some limited of HOBr-selective probes have been designed, there was no probes reported capable of sensing of HOBr with lysosome-targetable ability and red-emitting ratiometric fluorescence. Herein, we presented a 1,8-naphthalimide-based fluorescent probe Lyso-NpSN for rapid detection of HOBr over a wide pH range with high selectivity over other reactive oxygen species and sensitivity, for the first time. Furthermore, the probe was found to be low cytotoxicity to cells and had enabled to visualize exogenous and endogenous HOBr in living cells.

Michael J Davies - One of the best experts on this subject based on the ideXlab platform.

  • Hypobromous Acid and bromamine production by neutrophils and modulation by superoxide
    Biochemical Journal, 2009
    Co-Authors: Anna L P Chapman, Revathy Senthilmohan, Anthony J Kettle, Ojia Skaff, Michael J Davies
    Abstract:

    MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate to their respective hypohalous Acids. We have investigated the generation of HOBr by human neutrophils in the presence of physiological concentrations of chloride and bromide. HOBr was trapped with taurine and detected by monitoring the bromination of 4-HPAA (4-hydroxyphenylacetic Acid). With 100 microM bromide and 140 mM chloride, neutrophils generated HOBr and it accounted for approx. 13% of the hypohalous Acids they produced. Addition of SOD (superoxide dismutase) doubled the amount of HOBr detected. Therefore we investigated the reaction of superoxide radicals with a range of bromamines and bromamides and found that superoxide radicals stimulated the decomposition of these species, with this occurring in a time- and dose-dependent manner. The protection afforded by SOD against such decay demonstrates that these processes are superoxide-radical-dependent. These data are consistent with neutrophils generating HOBr at sites of infection and inflammation. Both HOBr and bromamines/bromamides have the potential to react with superoxide radicals to form additional radicals that may contribute to inflammatory tissue damage.

  • hypothiocyanous Acid is a more potent inducer of apoptosis and protein thiol depletion in murine macrophage cells than hypochlorous Acid or Hypobromous Acid
    Biochemical Journal, 2008
    Co-Authors: Mitchell M Lloyd, David Van Reyk, Michael J Davies, Clare L Hawkins
    Abstract:

    Hypohalous Acids are generated by activated leucocytes, via the formation of H2O2 and the release of peroxidase enzymes (myeloperoxidase and eosinophil peroxidase). These species are important bactericidal agents, but HOCl (hypochlorous Acid) and HOBr (Hypobromous Acid) have also been implicated in tissue damage in a number of inflammatory diseases. HOSCN (hypothiocyanous Acid; cyanosulfenic Acid) is a milder, more thiol-specific, oxidant than HOCl or HOBr and as such may be a more potent inducer of cellular dysfunction due to selective targeting of critical thiol residues on proteins. In the present study, HOCl and HOBr are shown to react rapidly with macrophage (J774A.1) cells, resulting in a greater extent of cell lysis compared with HOSCN. However, HOSCN induces apoptosis and necrosis with greater efficacy, and at lower concentrations, than HOCl or HOBr. Apoptosis occurs in conjunction with an increased release of cytochrome c into the cytosol, but no associated increase in caspase activity. Similarly, apoptosis is observed on treating the cells in the presence of a caspase inhibitor, suggesting that it is mediated by a caspase-independent pathway. HOSCN oxidized protein thiols more efficiently than either HOCl or HOBr. The greater efficacy of HOSCN in inducing apoptosis is attributed to selective damage to critical mitochondrial membrane protein thiol groups, resulting in increased permeability and subsequent leakage of cytochrome c into the cytosol. This induction of damage by HOSCN may be of critical importance in people with elevated levels of SCN− (thiocyanate ions) arising from cigarette smoking, and plays a role in the pathologies associated with this biological insult. Abbreviations: AIF, apoptosis-inducing factor; Ac-DEVD-MCA, N-acetyl-Asp-Glu-Val-Asp-7-amino-4-methylcoumarylamide; DTNB, 5,5′-dithiobis-(2-nitrobenzoic Acid); endoG, endonuclease G; EPO, eosinophil peroxidase; HOBr, Hypobromous Acid; HOCl, hypochlorous Acid; HOSCN, hypothiocyanous Acid (cyanosulfenic Acid); IAF, 5-iodoacetamidofluorescein; LPO, lactoperoxidase; MCA, 7-amino-4-methylcoumarin; MPO, myeloperoxidase; SCN−, thiocyanate ions; TNB, 5-thio-2-nitrobenzoic Acid; Z-VAD-FMK, benzyloxycarbonyl-Val-Ala-DL-Asp-fluoromethylketone

  • hypothiocyanous Acid is a more potent inducer of apoptosis and protein thiol depletion in murine macrophage cells than hypochlorous Acid or Hypobromous Acid
    Biochemical Journal, 2008
    Co-Authors: Mitchell M Lloyd, David Van Reyk, Michael J Davies, Clare L Hawkins
    Abstract:

    Hypohalous Acids are generated by activated leucocytes, via the formation of H(2)O(2) and the release of peroxidase enzymes (myeloperoxidase and eosinophil peroxidase). These species are important bactericidal agents, but HOCl (hypochlorous Acid) and HOBr (Hypobromous Acid) have also been implicated in tissue damage in a number of inflammatory diseases. HOSCN (hypothiocyanous Acid; cyanosulfenic Acid) is a milder, more thiol-specific, oxidant than HOCl or HOBr and as such may be a more potent inducer of cellular dysfunction due to selective targeting of critical thiol residues on proteins. In the present study, HOCl and HOBr are shown to react rapidly with macrophage (J774A.1) cells, resulting in a greater extent of cell lysis compared with HOSCN. However, HOSCN induces apoptosis and necrosis with greater efficacy, and at lower concentrations, than HOCl or HOBr. Apoptosis occurs in conjunction with an increased release of cytochrome c into the cytosol, but no associated increase in caspase activity. Similarly, apoptosis is observed on treating the cells in the presence of a caspase inhibitor, suggesting that it is mediated by a caspase-independent pathway. HOSCN oxidized protein thiols more efficiently than either HOCl or HOBr. The greater efficacy of HOSCN in inducing apoptosis is attributed to selective damage to critical mitochondrial membrane protein thiol groups, resulting in increased permeability and subsequent leakage of cytochrome c into the cytosol. This induction of damage by HOSCN may be of critical importance in people with elevated levels of SCN(-) (thiocyanate ions) arising from cigarette smoking, and plays a role in the pathologies associated with this biological insult.

  • kinetics of Hypobromous Acid mediated oxidation of lipid components and antioxidants
    Chemical Research in Toxicology, 2007
    Co-Authors: Ojia Skaff, David I Pattison, Michael J Davies
    Abstract:

    Hypohalous Acids are generated from the oxidation of halide ions by myeloperoxidase and eosinophil peroxidase in the presence of H2O2. These oxidants are potent antibacterial agents, but excessive production can result in host tissue damage, with this implicated in a number of human pathologies. Rate constants for HOCl with lipid components and antioxidants have been established. Here, the corresponding reactions of HOBr have been examined to determine whether this species shows similar reactivity. The second-order rate constants for the reaction of HOBr with 3-pentenoic Acid and sorbate, models of unsaturated lipids, are 1.1 × 104 and 1.3 × 103 M−1 s−1, respectively, while those for reaction of HOBr with phosphoryl-serine and phosphoryl-ethanolamine are ca. 106 M−1 s−1. The second-order rate constants (M−1 s−1) for reactions of HOBr with Trolox (6.4 × 104), hydroquinone (2.4 × 105), and ubiquinol-0 (2.5 × 106) were determined, as models of the lipid-soluble antioxidants, α-tocopherol, and ubiquinol-10; a...

  • degradation of extracellular matrix and its components by Hypobromous Acid
    Biochemical Journal, 2007
    Co-Authors: Martin D Rees, Michael J Davies, Tane N Mcniven
    Abstract:

    EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (Hypobromous Acid). They are released extracellularly by activated leucocytes and their binding to the polyanionic glycosa-minoglycan components of extracellular matrix (proteoglycans and hyaluronan) may localize the production of HOBr to these materials. It is shown in the present paper that the reaction of HOBr with glycosaminoglycans (heparan sulfate, heparin, chondroitin sulfate and hyaluronan) generates polymer-derived N-bromo derivatives (bromamines, dibromamines, N-bromosulfon-amides and bromamides). Decomposition of these species, which can occur spontaneously and/or via one-electron reduction by low-valent transition metal ions (Cu+ and Fe2+), results in polymer fragmentation and modification. One-electron reduction of the N-bromo derivatives generates radicals that have been detected by EPR spin trapping. The species detected are consistent with metal ion-dependent polymer fragmentation and modification being initiated by the formation of nitrogen-centred (aminyl, N-bromoaminyl, sulfonamidyl and amidyl) radicals. Previous studies have shown that the reaction of HOBr with proteins generates N-bromo derivatives and results in fragmentation of the polypeptide backbone. The reaction of HOBr with extracellular matrix synthesized by smooth muscle cells in vitro induces the release of carbohydrate and protein components in a time-dependent manner, which is consistent with fragmentation of these materials via the formation of N-bromo derivatives. The degradation of extracellular matrix glycosaminoglycans and proteins by HOBr may contribute to tissue damage associated with inflammatory diseases such as asthma.

Clare L Hawkins - One of the best experts on this subject based on the ideXlab platform.

  • hypothiocyanous Acid is a more potent inducer of apoptosis and protein thiol depletion in murine macrophage cells than hypochlorous Acid or Hypobromous Acid
    Biochemical Journal, 2008
    Co-Authors: Mitchell M Lloyd, David Van Reyk, Michael J Davies, Clare L Hawkins
    Abstract:

    Hypohalous Acids are generated by activated leucocytes, via the formation of H2O2 and the release of peroxidase enzymes (myeloperoxidase and eosinophil peroxidase). These species are important bactericidal agents, but HOCl (hypochlorous Acid) and HOBr (Hypobromous Acid) have also been implicated in tissue damage in a number of inflammatory diseases. HOSCN (hypothiocyanous Acid; cyanosulfenic Acid) is a milder, more thiol-specific, oxidant than HOCl or HOBr and as such may be a more potent inducer of cellular dysfunction due to selective targeting of critical thiol residues on proteins. In the present study, HOCl and HOBr are shown to react rapidly with macrophage (J774A.1) cells, resulting in a greater extent of cell lysis compared with HOSCN. However, HOSCN induces apoptosis and necrosis with greater efficacy, and at lower concentrations, than HOCl or HOBr. Apoptosis occurs in conjunction with an increased release of cytochrome c into the cytosol, but no associated increase in caspase activity. Similarly, apoptosis is observed on treating the cells in the presence of a caspase inhibitor, suggesting that it is mediated by a caspase-independent pathway. HOSCN oxidized protein thiols more efficiently than either HOCl or HOBr. The greater efficacy of HOSCN in inducing apoptosis is attributed to selective damage to critical mitochondrial membrane protein thiol groups, resulting in increased permeability and subsequent leakage of cytochrome c into the cytosol. This induction of damage by HOSCN may be of critical importance in people with elevated levels of SCN− (thiocyanate ions) arising from cigarette smoking, and plays a role in the pathologies associated with this biological insult. Abbreviations: AIF, apoptosis-inducing factor; Ac-DEVD-MCA, N-acetyl-Asp-Glu-Val-Asp-7-amino-4-methylcoumarylamide; DTNB, 5,5′-dithiobis-(2-nitrobenzoic Acid); endoG, endonuclease G; EPO, eosinophil peroxidase; HOBr, Hypobromous Acid; HOCl, hypochlorous Acid; HOSCN, hypothiocyanous Acid (cyanosulfenic Acid); IAF, 5-iodoacetamidofluorescein; LPO, lactoperoxidase; MCA, 7-amino-4-methylcoumarin; MPO, myeloperoxidase; SCN−, thiocyanate ions; TNB, 5-thio-2-nitrobenzoic Acid; Z-VAD-FMK, benzyloxycarbonyl-Val-Ala-DL-Asp-fluoromethylketone

  • hypothiocyanous Acid is a more potent inducer of apoptosis and protein thiol depletion in murine macrophage cells than hypochlorous Acid or Hypobromous Acid
    Biochemical Journal, 2008
    Co-Authors: Mitchell M Lloyd, David Van Reyk, Michael J Davies, Clare L Hawkins
    Abstract:

    Hypohalous Acids are generated by activated leucocytes, via the formation of H(2)O(2) and the release of peroxidase enzymes (myeloperoxidase and eosinophil peroxidase). These species are important bactericidal agents, but HOCl (hypochlorous Acid) and HOBr (Hypobromous Acid) have also been implicated in tissue damage in a number of inflammatory diseases. HOSCN (hypothiocyanous Acid; cyanosulfenic Acid) is a milder, more thiol-specific, oxidant than HOCl or HOBr and as such may be a more potent inducer of cellular dysfunction due to selective targeting of critical thiol residues on proteins. In the present study, HOCl and HOBr are shown to react rapidly with macrophage (J774A.1) cells, resulting in a greater extent of cell lysis compared with HOSCN. However, HOSCN induces apoptosis and necrosis with greater efficacy, and at lower concentrations, than HOCl or HOBr. Apoptosis occurs in conjunction with an increased release of cytochrome c into the cytosol, but no associated increase in caspase activity. Similarly, apoptosis is observed on treating the cells in the presence of a caspase inhibitor, suggesting that it is mediated by a caspase-independent pathway. HOSCN oxidized protein thiols more efficiently than either HOCl or HOBr. The greater efficacy of HOSCN in inducing apoptosis is attributed to selective damage to critical mitochondrial membrane protein thiol groups, resulting in increased permeability and subsequent leakage of cytochrome c into the cytosol. This induction of damage by HOSCN may be of critical importance in people with elevated levels of SCN(-) (thiocyanate ions) arising from cigarette smoking, and plays a role in the pathologies associated with this biological insult.

  • the role of aromatic amino Acid oxidation protein unfolding and aggregation in the Hypobromous Acid induced inactivation of trypsin inhibitor and lysozyme
    Chemical Research in Toxicology, 2005
    Co-Authors: Clare L Hawkins, Michael J Davies
    Abstract:

    Hypobromous Acid (HOBr) generated by activated eosinophils has been implicated in tissue injury observed in asthma, allergic reactions, and some infections. Proteins are major targets for this oxidant, but the mechanisms by which HOBr induces loss of function are not well-established. In this study, we have examined the effect of HOBr on protein structure (as assessed by amino Acid loss, side chain oxidation, fragmentation, aggregation, and unfolding) and activity of a model protease inhibitor, soybean trypsin inhibitor (STI), and the protective enzyme lysozyme. Exposure of both proteins to low oxidant concentrations (≤5-fold molar excess) results in loss of function. In each case, loss of activity is associated with the selective oxidation of His, Trp, and Tyr residues, which results in protein unfolding (with lysozyme) and protein aggregation (with STI). Reaction with these residues accounts for 25 and 50% of the HOBr with STI (25-fold excess) and lysozyme (4-fold excess), respectively. These processes ...

  • the role of reactive n bromo species and radical intermediates in Hypobromous Acid induced protein oxidation
    Free Radical Biology and Medicine, 2005
    Co-Authors: Clare L Hawkins, Michael J Davies
    Abstract:

    Activated eosinophils, and Hypobromous Acid (HOBr) generated by these cells, have been implicated in the tissue injury in asthma, allergic reactions, and some infections. Proteins are major targets for this oxidant, but limited information is available on the mechanisms of damage and intermediates formed. Reaction of HOBr with proteins is shown to result in the formation of bromamines and bromamides, from side-chain and backbone amines and amides, and 3-bromo- and 3,5-dibromo-Tyr, from Tyr residues; these materials account for ca. 70% of the oxidant consumed. Protein carbonyls, dityrosine, and 3,4-dihydroxyphenylalanine are also formed, though these are minor products (<5% of HOBr added). With BSA, extensive (selective and nonspecific) protein fragmentation and limited aggregation are also observed. The bromamines/bromamides are unstable and induce further oxidation and free radical formation as detected by EPR spin trapping. Evidence was obtained for the generation of nitrogen-centered radicals on side-chain and backbone amide groups of amino Acids, peptides, and proteins. These radicals readily undergo rearrangement reactions to give carbon-centered radicals. With proteins, alpha-carbon (backbone) radicals are detected, which may play a role in protein fragmentation. A novel damage transfer pathway from Gln side-chain amide groups to backbone sites was also observed.

Dongrui Luan - One of the best experts on this subject based on the ideXlab platform.

  • cyclic regulation of the sulfilimine bond in peptides and nc1 hexamers via the hobr h2se conjugated system
    Analytical Chemistry, 2018
    Co-Authors: Dongrui Luan, Aishan Zheng, Fanpeng Kong, Kehua Xu, Xiaoxiao Song, Bo Tang
    Abstract:

    The sulfilimine bond (−S═N−), found in the collagen IV scaffold, significantly stabilizes the architecture via the formation of sulfilimine cross-links. However, precisely governing the formation and breakup process of the sulfilimine bond in living organisms for better life functions still remains a challenge. Hence, we established a new way to regulate the breaking and formation of the sulfilimine bond through hydrogen selenide (H2Se) and Hypobromous Acid (HOBr), which can be easily controlled at simulated physiological conditions. This novel strategy provides a circulation regulation system to modulate the sulfilimine bond in peptides and NC1 hexamers, which can offer a substantial system for further study of the physiological function of collagen IV.

  • Cyclic Regulation of the Sulfilimine Bond in Peptides and NC1 Hexamers via the HOBr/H2Se Conjugated System
    2018
    Co-Authors: Dongrui Luan, Aishan Zheng, Fanpeng Kong, Xiaoxiao Song, Xiaojun Liu, Xiaonan Gao, Bo Tang
    Abstract:

    The sulfilimine bond (−SN−), found in the collagen IV scaffold, significantly stabilizes the architecture via the formation of sulfilimine cross-links. However, precisely governing the formation and breakup process of the sulfilimine bond in living organisms for better life functions still remains a challenge. Hence, we established a new way to regulate the breaking and formation of the sulfilimine bond through hydrogen selenide (H2Se) and Hypobromous Acid (HOBr), which can be easily controlled at simulated physiological conditions. This novel strategy provides a circulation regulation system to modulate the sulfilimine bond in peptides and NC1 hexamers, which can offer a substantial system for further study of the physiological function of collagen IV

  • high quantum yield mitochondria targeting near infrared fluorescent probe for imaging native Hypobromous Acid in living cells and in vivo
    Analytical Chemistry, 2017
    Co-Authors: Xiaojun Liu, Dongrui Luan, Aishan Zheng, Fanpeng Kong, Xiaoting Wang, Lili Tong, Bo Tang
    Abstract:

    The discovery that Hypobromous Acid (HOBr) can regulate the activity of collagen IV has attracted great attention. However, HOBr as an important reactive small molecule has hardly ever been studied using a detection method suitable for organisms. Herein, a high-quantum-yield mitochondria-targeting near-infrared (NIR) fluorescent probe for HOBr, RhSN-mito, was designed. RhSN-mito was easily obtained by the Suzuki cross-coupling reaction. The test results show that RhSN-mito can rapidly respond to HOBr with ultrasensitivity and high selectivity. The achievement of ultrasensitivity lies in the high signal-to-noise ratio and the highest fluorescence quantum yield of the reaction product (ΦF = 0.68) in the near-infrared region, as far as we know. RhSN-mito is successfully applied to image native HOBr in mitochondria of HepG2 cells and zebrafish. Thus, RhSN-mito is a powerful tool for detecting native HOBr in vivo and is expected to provide a method to further study the physiological and pathological functions ...

  • High-Quantum-Yield Mitochondria-Targeting Near-Infrared Fluorescent Probe for Imaging Native Hypobromous Acid in Living Cells and in Vivo
    2017
    Co-Authors: Xiaojun Liu, Dongrui Luan, Aishan Zheng, Fanpeng Kong, Xiaoting Wang, Lili Tong, Bo Tang
    Abstract:

    The discovery that Hypobromous Acid (HOBr) can regulate the activity of collagen IV has attracted great attention. However, HOBr as an important reactive small molecule has hardly ever been studied using a detection method suitable for organisms. Herein, a high-quantum-yield mitochondria-targeting near-infrared (NIR) fluorescent probe for HOBr, RhSN-mito, was designed. RhSN-mito was easily obtained by the Suzuki cross-coupling reaction. The test results show that RhSN-mito can rapidly respond to HOBr with ultrasensitivity and high selectivity. The achievement of ultrasensitivity lies in the high signal-to-noise ratio and the highest fluorescence quantum yield of the reaction product (ΦF = 0.68) in the near-infrared region, as far as we know. RhSN-mito is successfully applied to image native HOBr in mitochondria of HepG2 cells and zebrafish. Thus, RhSN-mito is a powerful tool for detecting native HOBr in vivo and is expected to provide a method to further study the physiological and pathological functions related to HOBr