The soluble curcumin derivative NDS27 inhibits superoxide anion production by neutrophils and acts as substrate and reversible inhibitor of myeloperoxidase
The soluble curcumin derivative NDS27 inhibits superoxide anion production by neutrophils and acts as substrate and reversible inhibitor of myeloperoxidase | Elsevier Enhanced Reader.pdf
Franck, Thierry ; Université de Liège - ULiège > Centre de l'oxygène : Recherche et développement (C.O.R.D.)
Aldib, I.; Laboratory of Pharmaceutical Chemistry & Analytical Platform of the Faculty of Pharmacy, Faculty of Pharmacy, Université Libre de Bruxelles, Brussels, Belgium
Zouaoui Boudjeltia, K.; Laboratory of Experimental Medicine, Université Libre de Bruxelles (ULB 222), CHU de Charleroi, Hôpital Vésale, Montigny-le-Tilleul, Belgium
Furtmüller, P. G.; Department of Chemistry, Division of Biochemistry, BOKU, University of Natural Resources and Life Sciences, Vienna, Austria
Obinger, C.; Department of Chemistry, Division of Biochemistry, BOKU, University of Natural Resources and Life Sciences, Vienna, Austria
NEVEN, Patricia ; Centre Hospitalier Universitaire de Liège - CHU > Département des Services Logistiques > Secteur entretien
Prévost, M.; Structure and Function of Biological Membranes, Faculty of Sciences, Université Libre de Bruxelles, Brussels, Belgium
Soubhye, J.; Laboratory of Pharmaceutical Chemistry & Analytical Platform of the Faculty of Pharmacy, Faculty of Pharmacy, Université Libre de Bruxelles, Brussels, Belgium
Van Antwerpen, P.; Laboratory of Pharmaceutical Chemistry & Analytical Platform of the Faculty of Pharmacy, Faculty of Pharmacy, Université Libre de Bruxelles, Brussels, Belgium
Mouithys-Mickalad, Ange ; Université de Liège - ULiège > Centre de l'oxygène : Recherche et développement (C.O.R.D.)
Serteyn, Didier ; Université de Liège - ULiège > Dép. clinique des animaux de compagnie et des équidés (DCA) > Anesthésiologie gén. et pathologie chirurg. des grds animaux
Language :
English
Title :
The soluble curcumin derivative NDS27 inhibits superoxide anion production by neutrophils and acts as substrate and reversible inhibitor of myeloperoxidase
Unlu, A., Nayir, E., Dogukan Kalenderoglu, M., Kirca, O., Ozdogan, M., Curcumin (Turmeric) and cancer. J. Buon. 21 (2016), 1050–1060.
Maheshwari, R.K., Singh, A.K., Gaddipati, J., Srimal, R.C., Multiple biological activities of curcumin: a short review. Life Sci. 78 (2006), 2081–2087.
Stanić Z., Curcumin, a compound from natural sources, a true scientific challenge - a review. Plant Foods Hum. Nutr. 72 (2017), 1–12.
Schneider, C., Gordon, O.N., Edwards, R.L., Luis, P.B., Degradation of curcumin: from mechanism to biological implications. J. Agric. Food Chem. 63 (2015), 7606–7614.
Cavaleri, F., Jia, W., The true nature of curcumin's polypharmacology. J. Prev. Med., 2, 2017, 5.
Neven, P., Serteyn, D., Delarge, J., Kiss, R., Mathieu, V., Cataldo, D., Rocks, N., World intellectual property organization. International Publication number WO/2009/144220 A1: Water soluble curcumin compositions for use in anticancer and anti-inflammatory therapy http://www.wipo.int/patentscope/search/en/WO2009144220, 2009. (Accessed 13 July 2011)
Kato, Y., Nagao, A., Terao, J., Osawa, T., Inhibition of myeloperoxidase-catalyzed tyrosylation by phenolic antioxidants in vitro. Biosci. Biotechnol. Biochem. 67 (2003), 1136–1139.
Franck, T., Kohnen, S., Grulke, S., Neven, P., Goutman, Y., Péters, F., Pirotte, B., Deby-Dupont, G., Serteyn, D., Inhibitory effect of curcuminoids and tetrahydrocurcuminoids on equine activated neutrophils and myeloperoxidase activity. Physiol. Res. 57 (2008), 577–587.
Drábiková K., Perečko, T., Nosáľ R., Harmatha, J., Smidrkal, J., Jančinová V., Polyphenol derivatives - potential regulators of neutrophil activity. Interdiscipl. Toxicol. 5 (2012), 65–70.
Derochette, S., Franck, T., Mouithys-Mickalad, A., Deby-Dupont, G., Neven, P., Serteyn, D., Intra- and extracellular antioxidant capacities of the new water-soluble form of curcumin (NDS27) on stimulated neutrophils and HL-60 cells. Chem. Biol. Interact. 201 (2013), 49–57.
Derochette, S., Mouithys-Mickalad, A., Franck, T., Collienne, S., Ceusters, J., Deby-Dupont, G., Neven, P., Serteyn, D., NDS27 combines the effect of curcumin lysinate and hydroxypropyl-β-cyclodextrin to inhibit equine PKCδ and NADPH oxidase involved in the oxidative burst of neutrophils. FEBS Open Bio. 4 (2014), 1021–1029.
Sandersen, C., Bienzle, D., Cerri, S., Franck, T., Derochette, S., Neven, P., Mouytis-Mickalad, A., Serteyn, D., Effect of inhaled hydrosoluble curcumin on inflammatory markers in broncho-alveolar lavage fluid of horses with LPS-induced lung neutrophilia. Multidiscip. Respir. Med., 10, 2015, 16.
Luis, P.B., Gordon, O.N., Nakashima, F., Joseph, A.I., Shibata, T., Uchida, K., Schneider, C., Oxidative metabolism of curcumin-glucuronide by peroxidases and isolated human leukocytes. Biochem. Pharmacol. 132 (2017), 143–149.
Pycock, J.F., Allen, W.E., Morris, T.H., Rapid, single-step isolation of equine neutrophils on a discontinuous Percoll density gradient. Res. Vet. Sci. 42 (1987), 411–412.
Franck, T., Minguet, G., Delporte, C., Derochette, S., Zouaoui Boudjeltia, K., Van Antwerpen, P., Gach, O., Deby-Dupont, G., Mouithys-Mickalad, A., Serteyn, D., An immunological method to combine the measurement of active and total myeloperoxidase on the same biological fluid, and its application in finding inhibitors which interact directly with the enzyme. Free Radic. Res. 49 (2015), 790–799.
Van Antwerpen, P., Prévost, M., Zouaoui-Boudjeltia, K., Babar, S., Legssyer, I., Moreau, P., Moguilevsky, N., Vanhaeverbeek, M., Ducobu, J., Nève, J., Dufrasne, F., Conception of myeloperoxidase inhibitors derived from flufenamic acid by computational docking and structure modification. Bioorg. Med. Chem. 16 (2008), 1702–1720.
Soubhye, J., Aldib, I., Elfving, B., Gelbcke, M., Furtmüller, P.G., Podrecca, M., Conotte, R., Colet, J.M., Rousseau, A., Reye, F., Sarakbi, A., Vanhaeverbeek, M., Kauffmann, J.M., Obinger, C., Nève, J., Prévost, M., Zouaoui Boudjeltia, K., Dufrasne, F., Van Antwerpen, P., Design, synthesis, and structure-activity relationship studies of novel 3-alkylindole derivatives as selective and highly potent myeloperoxidase inhibitors. J. Med. Chem. 56 (2013), 3943–3958.
Furtmüller, P.G., Burner, U., Obinger, C., Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate. Biochemistry 37 (1998), 17923–17930.
Forbes, L.V., Sjögren, T., Auchère, F., Jenkins, D.W., Thong, B., Laughton, D., Hemsley, P., Pairaudeau, G., Turner, R., Eriksson, H., Unitt, J.F., Kettle, A.J., Potent reversible inhibition of myeloperoxidase by aromatic hydroxamates. J. Biol. Chem. 288 (2013), 36636–36647.
Jurenka, J.S., Anti-inflammatory properties of curcumin, a major constituent of Curcuma longa: a review of preclinical and clinical research- A review. Altern. Med. Rev. 14 (2009), 141–153.
Fan, X., Zhang, C., Liu, D.B., Yan, J., Liang, H.P., The clinical applications of curcumin: current state and the future- A review. Curr. Pharmaceut. Des. 19 (2013), 2011–2031.
Sandersen, C., Olejnik, D., Franck, T., Neven, P., Serteyn, D., Art, T., Inhalation with NDS27 attenuates pulmonary neutrophilic inflammation in recurrent airway obstruction. Vet. Rec., 169, 2011, 100.
Feng, J.Y., Liu, Z.Q., Phenolic and enolic hydroxyl groups in curcumin: which plays the major role in scavenging radicals?. J. Agric. Food Chem. 57 (2009), 11041–11046.
Zheng, Q.T., Yang, Z.H., Yu, L.Y., Ren, Y.Y., Huang, Q.X., Liu, Q., Ma, X.Y., Chen, Z.K., Wang, Z.B., Zheng, X., Synthesis and antioxidant activity of curcumin analogs. J. Asian Nat. Prod. Res. 19 (2017), 489–503.
Morales, N.P., Sirijaroonwong, S., Yamanont, P., Phisalaphong, C., Electron paramagnetic resonance study of the free radical scavenging capacity of curcumin and its demethoxy and hydrogenated derivatives. Biol. Pharm. Bull. 38 (2015), 1478–1483.
Arnhold, J., Monzani, E., Furtmüller, P.G., Zederbauer, M., Casella, L., Obinger, C., Kinetics and thermodynamics of halide and nitrite oxidation by mammalian heme peroxidases. Eur. J. Inorg. Chem. 19 (2006), 3801–3811.
Battistuzzi, G., Stampler, J., Bellei, M., Vlasits, J., Soudi, M., Furtmüller, P.G., Obinger, C., Influence of the covalent heme-protein bonds on the redox thermodynamics of human myeloperoxidase. Biochemistry 50 (2011), 7987–7994.
Furtmüller, P.G., Burner, U., Obinger, C., Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate. Biochemistry 37 (1998), 17923–17930.
Zederbauer, M., Furtmüller, P.G., Brogioni, S., Jakopitsch, C., Smulevich, G., Obinger, C., Heme to protein linkages in mammalian peroxidases: impact on spectroscopic, redox and catalytic properties-A review. Nat. Prod. Rep. 24 (2007), 571–584.
Malle, E., Furtmüller, P.G., Sattler, W., Obinger, C., Myeloperoxidase: a target for new drug development?. Br. J. Pharmacol. 152 (2007), 838–854.
Van Antwerpen, P., Zouaoui Boudjeltia, K., Rational drug design applied to myeloperoxidase inhibition. Free Radic. Res. 49 (2015), 711–720.
Nussbaum, C., Klinke, A., Adam, M., Baldus, S., Sperandio, M., Myeloperoxidase: a leukocyte-derived protagonist of inflammation and cardiovascular disease. Antioxidants Redox Signal. 18 (2013), 692–713.
Kharat, M., Du, Z., Zhang, G., McClements, D.J., Physical and chemical stability of curcumin in aqueous solutions and emulsions: impact of pH, temperature, and molecular environment. J. Agric. Food Chem. 65 (2017), 1525–1532.
Burner, U., Furtmuller, P.G., Kettle, A.J., Koppenol, W.H., Obinger, C., Mechanism of reaction of myeloperoxidase with nitrite. J. Biol. Chem. 275 (2000), 20597–20601.
Nève, J., Parij, N., Moguilevsky, N., Inhibition of the myeloperoxidase chlorinating activity by non-steroidal anti-inflammatory drugs investigated with a human recombinant enzyme. Eur. J. Pharmacol. 417 (2001), 37–43.
Furtmüller, P.G., Arnhold, J., Jantschko, W., Pichler, H., Obinger, C., Redox properties of the couples compound I/compound II and compound II/native enzyme of human myeloperoxidase. Biochem. Biophys. Res. Commun. 301 (2003), 551–557.
Aldib, I., Soubhye, J., Zouaoui Boudjeltia, K., Vanhaeverbeek, M., Rousseau, A., Furtmüller, P.G., Obinger, C., Dufrasne, F., Nève, J., Van Antwerpen, P., Prévost, M., Evaluation of new scaffolds of myeloperoxidase inhibitors by rational design combined with high-throughput virtual screening. J. Med. Chem. 55 (2012), 7208–7218.
Aldib, I., Gelbcke, M., Soubhye, J., Prévost, M., Furtmüller, P.G., Obinger, C., Elfving, B., Alard, I.C., Roos, G., Delporte, C., Berger, G., Dufour, D., Zouaoui Boudjeltia, K., Nève, J., Dufrasne, F., Van Antwerpen, P., Novel bis-arylalkylamines as myeloperoxidase inhibitors: design, synthesis, and structure-activity relationship study. Eur. J. Med. Chem. 123 (2016), 746–762.
Singh, R., Tønnesen, H.H., Vogensen, S.B., Loftsson, T., Masson, M., Studies of curcumin and curcuminoids. XXXVI. The stoichiometry and complexation constants of cyclodextrin complexes as determined by the phase-solubility method and UV–Vis titration. J. Inclusion Phenom. Macrocycl. Chem. 66 (2010), 335–348.
Ouyang, H.Z., Fang, L., Zhu, L., Zhang, L., Ren J He, X.L., Qi, A.D., Effect of external factors on the curcumin/2-hydroxypropyl- b-cyclodextrin: in vitro and in vivo study. J. Inclusion Phenom. Macrocycl. Chem. 73 (2012), 423–433.
Shityakov, S., Salmas, R.E., Durdagi, S., Roewer, N., Förster, C., Broscheit, J., Solubility profiles, hydration and desolvation of curcumin complexed with γ-cyclodextrin and hydroxypropyl-γ-cyclodextrin. J. Mol. Struct. 1134 (2017), 91–98.
Hegge, A.B., Másson, M., Kristensen, S., Tønnesen, H.H., Investigation of curcumin-cyclodextrin inclusion complexation in aqueous solutions containing various alcoholic co-solvents and alginates using an UV-VIS titration method. Studies of curcumin and curcuminoides, XXXV. Pharmazie 64 (2009), 382–389.
