메뉴 건너뛰기




Volumn 51, Issue 22, 2008, Pages 7313-7317

Antithyroid drug carbimazole and its analogues: Synthesis and inhibition of peroxidase-catalyzed iodination of L-tyrosine

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOLYTE; ANTITHYROID AGENT; CARBIMAZOLE; DISULFIDE; PEROXIDASE; SELENIUM DERIVATIVE; THIAMAZOLE; TYROSINE;

EID: 56749107425     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm800894m     Document Type: Article
Times cited : (23)

References (35)
  • 1
    • 0041735276 scopus 로고    scopus 로고
    • Hyperthyroidism
    • (a) Cooper, D. S. Hyperthyroidism. Lancet 2003, 362, 459-468.
    • (2003) Lancet , vol.362 , pp. 459-468
    • Cooper, D.S.1
  • 2
    • 14544296973 scopus 로고    scopus 로고
    • Antithyroid drugs
    • and references therein
    • (b) Cooper, D. S. Antithyroid drugs. N. Engl. J. Med. 2005, 352, 905-917, and references therein.
    • (2005) N. Engl. J. Med , vol.352 , pp. 905-917
    • Cooper, D.S.1
  • 3
    • 0017254963 scopus 로고
    • The mechanism of action of the thioureylene antithyroid drugs
    • (a) Taurog, A. The mechanism of action of the thioureylene antithyroid drugs. Endocrinology 1976, 98, 1031-1046.
    • (1976) Endocrinology , vol.98 , pp. 1031-1046
    • Taurog, A.1
  • 4
    • 0018075631 scopus 로고
    • The irreversible inactivation of thyroid peroxidase by methylmercaptoimidazole, thiouracil, and propylthiouracil in vitro and its relationship to in vivo findings
    • (b) Davidson, B.; Soodak, M.; Neary, J. T.; Strout, H. V.; Kieffer, J. D.; Mover, H.; Maloof, F. The irreversible inactivation of thyroid peroxidase by methylmercaptoimidazole, thiouracil, and propylthiouracil in vitro and its relationship to in vivo findings. Endocrinology 1978, 103, 871-882.
    • (1978) Endocrinology , vol.103 , pp. 871-882
    • Davidson, B.1    Soodak, M.2    Neary, J.T.3    Strout, H.V.4    Kieffer, J.D.5    Mover, H.6    Maloof, F.7
  • 5
    • 0020687748 scopus 로고
    • Reversible and irreversible inhibition of thyroid peroxidase-catalyzed iodination by thioureylene drugs
    • (c) Engler, H.; Taurog, A.; Luthy, C.; Dorris, M. L. Reversible and irreversible inhibition of thyroid peroxidase-catalyzed iodination by thioureylene drugs. Endocrinology 1983, 112, 86-95.
    • (1983) Endocrinology , vol.112 , pp. 86-95
    • Engler, H.1    Taurog, A.2    Luthy, C.3    Dorris, M.L.4
  • 6
    • 0020559777 scopus 로고
    • Mechanism of action of thioureylene antithyroid drugs in the rat: Possible inactivation of thyroid peroxidase by propylthiouracil
    • (d) Shiroozu, A.; Taurog, A.; Engler, H.; Dorris, M. L. Mechanism of action of thioureylene antithyroid drugs in the rat: possible inactivation of thyroid peroxidase by propylthiouracil. Endocrinology 1983, 113, 362-370.
    • (1983) Endocrinology , vol.113 , pp. 362-370
    • Shiroozu, A.1    Taurog, A.2    Engler, H.3    Dorris, M.L.4
  • 7
    • 0038501459 scopus 로고    scopus 로고
    • It has been reported that PTU, but not MMI, also inhibits the selenocysteine-containing enzyme iodothyronine deiodinase (ID, which catalyzes the monodeiodination of the prohormone thyroxine (T4) to its biologically active form T3. For details, see: (a) Köhrle, J. The trace element seienium and the thyroid gland. Biochimie 1999, 81, 527-533
    • It has been reported that PTU, but not MMI, also inhibits the selenocysteine-containing enzyme iodothyronine deiodinase (ID), which catalyzes the monodeiodination of the prohormone thyroxine (T4) to its biologically active form T3. For details, see: (a) Köhrle, J. The trace element seienium and the thyroid gland. Biochimie 1999, 81, 527-533.
  • 8
    • 0035796663 scopus 로고    scopus 로고
    • Reactions of organoselenenyl iodides with thiouracil drugs: An enzyme mimetic study on the inhibition of iodothyronine deiodinase
    • (b) du Mont, W.-W.; Mugesh, G.; Wismach, C.; Jones, P. G. Reactions of organoselenenyl iodides with thiouracil drugs: an enzyme mimetic study on the inhibition of iodothyronine deiodinase. Angew. Chem., Int. Ed. 2001, 40, 2486-2489.
    • (2001) Angew. Chem., Int. Ed , vol.40 , pp. 2486-2489
    • du Mont, W.-W.1    Mugesh, G.2    Wismach, C.3    Jones, P.G.4
  • 9
    • 0036191639 scopus 로고    scopus 로고
    • Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases
    • (c) Bianco, A. C.; Salvatore, D.; Gereben, B.; Berry, M. J.; Larsen, P. R. Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases. Endocr. Rev. 2002, 23, 38-89.
    • (2002) Endocr. Rev , vol.23 , pp. 38-89
    • Bianco, A.C.1    Salvatore, D.2    Gereben, B.3    Berry, M.J.4    Larsen, P.R.5
  • 10
    • 0036125773 scopus 로고    scopus 로고
    • Iodothyronine deiodinases
    • (d) Köhrle, J. Iodothyronine deiodinases. Methods Enzymol. 2002, 347, 125-167.
    • (2002) Methods Enzymol , vol.347 , pp. 125-167
    • Köhrle, J.1
  • 11
    • 0018597527 scopus 로고
    • Rapid conversion of carbimazole to methimazole in serum; evidence for an enzymatic mechanism
    • (a) Nakashima, T.; Tourog, A. Rapid conversion of carbimazole to methimazole in serum; evidence for an enzymatic mechanism. Clin. Endocrinol. 1979, 10, 637-648.
    • (1979) Clin. Endocrinol , vol.10 , pp. 637-648
    • Nakashima, T.1    Tourog, A.2
  • 13
    • 0027051113 scopus 로고
    • Selenoracil derivatives are potent inhibitors of the selenoenzyme type I iodothyronine deiodinase
    • (a) Visser, T. J.; Kaptein, E.; Aboul-Enein, H. Y. Selenoracil derivatives are potent inhibitors of the selenoenzyme type I iodothyronine deiodinase. Biochem. Biophys. Res. Commun. 1992, 189, 1362-1367.
    • (1992) Biochem. Biophys. Res. Commun , vol.189 , pp. 1362-1367
    • Visser, T.J.1    Kaptein, E.2    Aboul-Enein, H.Y.3
  • 14
    • 0027380292 scopus 로고
    • Synthesis and the antiperoxidase activity of seleno analogues of the antithyroid drug propylthiouracil
    • (b) Aboul-Enein, H. Y.; Awad, A. A.; Al-Andis, N. M. Synthesis and the antiperoxidase activity of seleno analogues of the antithyroid drug propylthiouracil. J. Enzyme. Inhib. 1993, 7, 147-150.
    • (1993) J. Enzyme. Inhib , vol.7 , pp. 147-150
    • Aboul-Enein, H.Y.1    Awad, A.A.2    Al-Andis, N.M.3
  • 15
    • 0027965163 scopus 로고
    • A directed metalation route to the selenium analog of methimazole
    • (c) Guziec, L. J.; Guziec, F. S. Jr. A directed metalation route to the selenium analog of methimazole. J. Org. Chem. 1994, 59, 4691-4692.
    • (1994) J. Org. Chem , vol.59 , pp. 4691-4692
    • Guziec, L.J.1    Guziec Jr., F.S.2
  • 16
    • 0027944003 scopus 로고
    • The selenium analog of methimazole. Measurement of its inhibitory effect on type I 5′-deiodinase and of its antithyroid activity
    • (d) Taurog, A.; Dorris, M. L.; Guziec, L. J.; Guziec, F. S., Jr. The selenium analog of methimazole. Measurement of its inhibitory effect on type I 5′-deiodinase and of its antithyroid activity. Biochem. Pharmacol. 1994, 48, 1447-1453.
    • (1994) Biochem. Pharmacol , vol.48 , pp. 1447-1453
    • Taurog, A.1    Dorris, M.L.2    Guziec, L.J.3    Guziec Jr., F.S.4
  • 17
    • 0028946498 scopus 로고
    • The selenium analog of 6-propylthiouracil. Measurement of its inhibitory effect on type I iodothyronine deiodinase and of its antithyroid activity
    • (e) Taurog, A.; Dorris, M. L.; Hu, W.-X.; Guziec, F. S. Jr. The selenium analog of 6-propylthiouracil. Measurement of its inhibitory effect on type I iodothyronine deiodinase and of its antithyroid activity. Biochem. Pharmacol. 1995, 49, 701-709.
    • (1995) Biochem. Pharmacol , vol.49 , pp. 701-709
    • Taurog, A.1    Dorris, M.L.2    Hu, W.-X.3    Guziec Jr., F.S.4
  • 18
    • 33749180636 scopus 로고    scopus 로고
    • Synthesis and structural characterization of 1-mesityl-1,3-dihydro- imidazole-2-selone and bis(1-mesitylimidazol-2-yl)diselenide: Experimental evidence that the selone is more stable than the selenol tautomer
    • (f) Landry, V. K.; Minoura, M.; Pang, K.; Buccella, D.; Kelly, B. V.; Parkin, G. Synthesis and structural characterization of 1-mesityl-1,3-dihydro- imidazole-2-selone and bis(1-mesitylimidazol-2-yl)diselenide: experimental evidence that the selone is more stable than the selenol tautomer. J. Am. Chem. Soc. 2006, 128, 12490-12497.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 12490-12497
    • Landry, V.K.1    Minoura, M.2    Pang, K.3    Buccella, D.4    Kelly, B.V.5    Parkin, G.6
  • 19
    • 33748556877 scopus 로고    scopus 로고
    • Synthesis and structures of Se analogues of the antithyroid drug 6-n-propyl-2-thiouracil and its alkyl derivatives: Formation of dimeric Se-Se compounds and deselenation reactions of charge-transfer adducts of diiodine
    • (g) Antoniadis, C. D.; Hadjikakou, S. K.; Hadjiliadis, N.; Papakyriakou, A.; Baril, M.; Butler, I. S. Synthesis and structures of Se analogues of the antithyroid drug 6-n-propyl-2-thiouracil and its alkyl derivatives: formation of dimeric Se-Se compounds and deselenation reactions of charge-transfer adducts of diiodine. Chem. - Eur. J. 2006, 12, 6888-6897.
    • (2006) Chem. - Eur. J , vol.12 , pp. 6888-6897
    • Antoniadis, C.D.1    Hadjikakou, S.K.2    Hadjiliadis, N.3    Papakyriakou, A.4    Baril, M.5    Butler, I.S.6
  • 20
    • 1542287649 scopus 로고    scopus 로고
    • Biomimetic studies on antithyroid drugs and thyroid hormone synthesis
    • (a) Roy, G.; Nethaji, M.; Mugesh, G. Biomimetic studies on antithyroid drugs and thyroid hormone synthesis. J. Am. Chem. Soc. 2004, 126, 2712-2713.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 2712-2713
    • Roy, G.1    Nethaji, M.2    Mugesh, G.3
  • 21
    • 84962338794 scopus 로고    scopus 로고
    • Antithyroid drugs and thyroid hormone synthesis: Effect of methimazole derivatives on peroxidase-catalyzed reactions
    • (b) Roy, G.; Mugesh, G. Antithyroid drugs and thyroid hormone synthesis: effect of methimazole derivatives on peroxidase-catalyzed reactions. J. Am. Chem. Soc. 2005, 127, 15207-15217.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 15207-15217
    • Roy, G.1    Mugesh, G.2
  • 22
    • 84961979106 scopus 로고    scopus 로고
    • Interaction of antithyroid drugs with iodine: The isolation of two unusual ionic compounds derived from Se-methimazole
    • (c) Roy, G.; Nethaji, M.; Mugesh, G. Interaction of antithyroid drugs with iodine: the isolation of two unusual ionic compounds derived from Se-methimazole. Org. Biomol. Chem. 2006, 4, 2883-2887.
    • (2006) Org. Biomol. Chem , vol.4 , pp. 2883-2887
    • Roy, G.1    Nethaji, M.2    Mugesh, G.3
  • 23
    • 33751535780 scopus 로고    scopus 로고
    • Bioinorganic chemistry aspects of the inhibition of thyroid hormone biosynthesis by antihyperthyroid drugs
    • (d) Roy, G.; Das, D.; Mugesh, G. Bioinorganic chemistry aspects of the inhibition of thyroid hormone biosynthesis by antihyperthyroid drugs. Inorg. Chim. Acta 2007, 360, 303-316.
    • (2007) Inorg. Chim. Acta , vol.360 , pp. 303-316
    • Roy, G.1    Das, D.2    Mugesh, G.3
  • 24
    • 45549109618 scopus 로고    scopus 로고
    • Selenium analogues of antithyroid drugs-recent developments
    • (e) Roy, G.; Mugesh, G. Selenium analogues of antithyroid drugs-recent developments. Chem. Biodiversity 2008, 5, 414-439.
    • (2008) Chem. Biodiversity , vol.5 , pp. 414-439
    • Roy, G.1    Mugesh, G.2
  • 27
    • 84943920736 scopus 로고
    • Phase annealing in SHELX-90: Direct methods for larger structures
    • (b) Sheldrick, G. M. Phase annealing in SHELX-90: direct methods for larger structures. Acta Crystallogr. Sect. A: Found. Crystallogr. 1990, 46, 467-473.
    • (1990) Acta Crystallogr. Sect. A: Found. Crystallogr , vol.46 , pp. 467-473
    • Sheldrick, G.M.1
  • 28
    • 56749139518 scopus 로고    scopus 로고
    • Sheldrick, G. M. SHELX-97, Program for the Refinement of Crystal Structures; University of Göttingen: Göttingen, Germany, 1997; CCDC-693450 (for compound 5), CCDC-693451 (for compound 15), CCDC-693452 (for compound 20), CCDC-693453 (for compound 14), and CCDC-693454 (for compound 6) contain the supplementary crystallographic data for this paper. These data can be obtained free of charge from The Cambridge Crystallographic Data Centre via www.ccdc.cam.ac.uk/data_request/cif.
    • (c) Sheldrick, G. M. SHELX-97, Program for the Refinement of Crystal Structures; University of Göttingen: Göttingen, Germany, 1997; CCDC-693450 (for compound 5), CCDC-693451 (for compound 15), CCDC-693452 (for compound 20), CCDC-693453 (for compound 14), and CCDC-693454 (for compound 6) contain the supplementary crystallographic data for this paper. These data can be obtained free of charge from The Cambridge Crystallographic Data Centre via www.ccdc.cam.ac.uk/data_request/cif.
  • 29
    • 56749171748 scopus 로고    scopus 로고
    • All the calculations were carried out by using the Gaussian suite of quantum chemical programs. Frisch, M. J, Trucks, G. W, Schlegel, H. B, Scusera, G. E, Robb, M. A, Cheeseman, J. R, Zakrzewski, V. G, Montgomery, J. A, Jr, Stratmann, R. E, Burant, J. C, Dapprich, S, Millam, J. M, Daniels, A. D, Kudin, K. N, Strain, M. C, Farkas, O, Tomasi, J, Barone, V, Cossi, M, Cammi, R, Mennucci, B, Pomelli, C, Adamo, C, Clifford, S, Ochterski, J, Petersson, G. A, Ayala, P. Y, Cui, Q, Morokuma, K, Malick, D. K, Rabuck, A. D, Raghavachari, K, Foresman, J. B, Cioslowski, J, Ortiz, J. V, Stefanov, B. B, Liu, G, Liashenko, A, Piskorz, P, Komaromi, I, Gomperts, R, Martin, R. L, Fox, D. J, Keith, T, Al-Laham, M. A, Peng, C. Y, Nanayakkara, A, Gonzalez, C, Challacombe, M, Gill, P. M. W, Johnson, B. G, Chen, W, Wong, M. W, Andres, J. L, Gonzale, C, Head-Gordon, M, Replogle, E. S, Pople, J. A. Gaussian 98, revision A 11.3; Gaussian, Inc, Pitt
    • All the calculations were carried out by using the Gaussian suite of quantum chemical programs. Frisch, M. J.; Trucks, G. W.; Schlegel, H. B.; Scusera, G. E.; Robb, M. A.; Cheeseman, J. R.; Zakrzewski, V. G.; Montgomery, J. A., Jr.; Stratmann, R. E.; Burant, J. C.; Dapprich, S.; Millam, J. M.; Daniels, A. D.; Kudin, K. N.; Strain, M. C.; Farkas, O.; Tomasi, J.; Barone, V.; Cossi, M.; Cammi, R.; Mennucci, B.; Pomelli, C.; Adamo, C.; Clifford, S.; Ochterski, J.; Petersson, G. A.; Ayala, P. Y.; Cui, Q.; Morokuma, K.; Malick, D. K.; Rabuck, A. D.; Raghavachari, K.; Foresman, J. B.; Cioslowski, J.; Ortiz, J. V.; Stefanov, B. B.; Liu, G.; Liashenko, A.; Piskorz, P.; Komaromi, I.; Gomperts, R.; Martin, R. L.; Fox, D. J.; Keith, T.; Al-Laham, M. A.; Peng, C. Y.; Nanayakkara, A.; Gonzalez, C.; Challacombe, M.; Gill, P. M. W.; Johnson, B. G.; Chen, W.; Wong, M. W.; Andres, J. L.; Gonzale, C.; Head-Gordon, M.; Replogle, E. S.; Pople, J. A. Gaussian 98, revision A 11.3; Gaussian, Inc.; Pittsburgh, PA, 1998.
  • 30
    • 0011083499 scopus 로고
    • Intermolecular interactions from a natural bond orbital, donor-acceptor viewpoint
    • (a) Reed, A. E.; Curtiss, L. A.; Weinhold, F. Intermolecular interactions from a natural bond orbital, donor-acceptor viewpoint. Chem. Rev. 1988, 88, 899-926.
    • (1988) Chem. Rev , vol.88 , pp. 899-926
    • Reed, A.E.1    Curtiss, L.A.2    Weinhold, F.3
  • 31
    • 56749090030 scopus 로고    scopus 로고
    • Glendening, E. D, Reed, J. E, Carpenter, J. E, Weinhold, F. Natural Bond Orbital NBO, version 3.1
    • (b) Glendening, E. D.; Reed, J. E.; Carpenter, J. E.; Weinhold, F. Natural Bond Orbital (NBO), version 3.1.
  • 32
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
    • (a) Lee, C.; Yang, W.; Parr, R. G. Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density. Phys. Rev. B 1988, 37, 785-789.
    • (1988) Phys. Rev. B , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 33
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • (b) Becke, A. D. Density-functional thermochemistry. III. The role of exact exchange. J. Chem. Phys. 1993, 98, 5648-5652.
    • (1993) J. Chem. Phys , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 34
    • 0016248790 scopus 로고    scopus 로고
    • The enzyme inhibition experiments were carried out with Fe-containing lactoperoxidase (LPO) because it is readily available in purified form. Furthermore, LPO has been shown to behave very similarly to TPO with respect to iodination of thyroglobulin, the natural substrate, and other iodide acceptors. Taurog, A.; Dorris, M. L.; Lamas, L. Comparison of lactoperoxidase- and thyroid peroxidase-catalyzed iodination and coupling. Endocrinology 1974, 94, 1286-1294.
    • The enzyme inhibition experiments were carried out with Fe-containing lactoperoxidase (LPO) because it is readily available in purified form. Furthermore, LPO has been shown to behave very similarly to TPO with respect to iodination of thyroglobulin, the natural substrate, and other iodide acceptors. Taurog, A.; Dorris, M. L.; Lamas, L. Comparison of lactoperoxidase- and thyroid peroxidase-catalyzed iodination and coupling. Endocrinology 1974, 94, 1286-1294.
  • 35
    • 56749145338 scopus 로고    scopus 로고
    • The hydrolysis of N-C bond in assay mixture was confirmed by HPLC analysis. The initial rates for the hydrolysis of N-C bond in various thiones/selones are given in Supporting Information, (Page S18).
    • The hydrolysis of N-C bond in assay mixture was confirmed by HPLC analysis. The initial rates for the hydrolysis of N-C bond in various thiones/selones are given in Supporting Information, (Page S18).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.