Anticancer steroid sulfatase inhibitors: synthesis of a potent fluorinated second-generation agent, in vitro and in vivo activities, molecular modeling, and protein crystallography (644 views)
Mol Cancer Ther (ISSN: 1535-7163, 1538-8514electronic), 2008 Sep; 7(8): 2435-2444.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.003, 5-year impact factor: 5.428
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-53349089862&partnerID=40&md5=4d4f3c49bf6a556109d89d26b4e5ea48
Keywords: 3 Hydroxy N 3, 3 Trifluoropropyl 16, 17 Seco Estra 1, 5(10) Triene 16, 17 Imide, 3 Sulfamoyloxy N 3, 667 Coumarin, Antineoplastic Agent, Estrone, Estrone 3 O Sulfamic Acid, Stx 64, Unclassified Drug, Animal Experiment, Animal Model, Antineoplastic Activity, Article, Binding Site, Breast Cancer, Controlled Study, Crystallization, Crystallography, Drug Synthesis, Female, Hydrogen Bond, Hydrophobicity, Molecular Model, Nonhuman, Priority Journal, Protein Interaction, Single Drug Dose, Chromatography, Liquid, X-Ray, Enzyme Inhibitors, Fluorine, Magnetic Resonance Spectroscopy, Protein Conformation, Wistar, Spectrometry, Electrospray Ionization, Steryl-Sulfatase, 5 (10) Triene 16,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy and Pharmacology, Sterix Ltd., University of Bath, Bath, United Kingdom
Department of Endocrinology and Metabolic Medicine, Imperial College London, St. Mary's Hospital, London, United Kingdom
Istituto di Biostrutture e Bioimmagini-CNR, Naples, Italy
Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Florence, Italy
Universit degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Florence, Italy
References:
Reed, M.J., Purohit, A., Woo, L.W.L., Newman, S.P., Potter, B.V.L., Steroid sulfatase: Molecular biology, regulation, and inhibition (2005) Endocr Rev, 26, pp. 171-20
Stanway, S.J., Purohit, A., Woo, L.W.L., Phase I study of STX 64 (667 Coumate) in breast cancer patients: The first study of a steroid sulfatase inhibitor (2006) Clin Cancer Res, 12, pp. 1585-1592
Elger, W., Schwarz, S., Hedden, A., Reddersen, G., Schneider, B., Sulfamates of various estrogens are prodrugs with increased systemic and reduced hepatic estrogenicity at oral application (1995) J Steroid Biochem Mol Biol, 55, pp. 395-403
Foster, P.A., Newman, S.P., Chander, S.K., In vivo efficacy of STX213, a second-generation steroid sulfatase inhibitor, for hormone-dependent breast cancer therapy (2006) Clin Cancer Res, 12, pp. 5543-5549
Foster, P.A., Chander, S.K., Parsons, M.F., Efficacy of three potent steroid sulfatase inhibitors: Pre-clinical investigations for their use in the treatment of hormone-dependent breast cancer (2008) Breast Cancer Res Treat, 111, pp. 129-138
Stanway, S.J., Delavault, P., Purohit, A., Steroid sulfatase: A new target for the endocrine therapy of breast cancer (2007) Oncologist, 12, pp. 370-374
Fischer, D.S., Woo, L.W.L., Mahon, M.F., Purohit, A., Reed, M.J., Potter, B.V.L., D-ring modified estrone derivatives as novel potent inhibitors of steroid sulfatase (2003) Bioorg Med Chem, 11, pp. 1685-1700
Fischer, D.S., Chander, S.K., Woo, L.W.L., Novel D-ring modified steroid derivatives as potent, non-estrogenic, steroid sulfatase inhibitors with in vivo activity (2003) J Steroid Biochem Mol Biol, 84, pp. 343-349
Purohit, A., Williams, G.J., Roberts, C.J., Potter, B.V.L., Reed, M.J., In vivo inhibition of oestrone sulphatase and dehydroepiandrosterone sulphatase by oestrone-3-O-sulphamate (1995) Int J Cancer, 63, pp. 106-111
Hernandez-Guzman, F.G., Higashiyama, T., Pangborn, W., Osawa, Y., Ghosh, D., Structure of human estrone sulfatase suggests functional roles of membrane association (2003) J Biol Chem, 278, pp. 22989-22997
Woo LWL, Lightowler M, Purohit A, Reed MJ, Potter BVL. Heteroatom-substituted analogues of the active-site directed inhibitor estra-1,3,5(10)-trien-17-one-3-sulphamate inhibit estrone sulphatase by a different mechanism. J Steroid Biochem Mol Biol 1996
57:79-88Jones, G., Willett, P., Glen, R.C., Leach, A.R., Taylor, R., Development and validation of a genetic algorithm for flexible docking (1997) J Mol Biol, 267, pp. 727-748
Eriksson, A.E., Jones, T.A., Liljas, A., Refined structure of human carbonic anhydrase II at 2.0 A resolution (1988) Proteins, 4, pp. 274-282
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol, 276, pp. 307-326
Brunger, A.T., Adams, P.D., Clore, G.M., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr D Biol Crystallogr, 54, pp. 905-921
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr A, 47, pp. 110-119
Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK - a program to check the stereochemical quality of protein structures (1993) J Appl Crystallogr, 26, pp. 283-291
Park, B.K., Kitteringham, N.R., O'Neill, P.M., Metabolism of fluorine-containing drugs (2001) Annu Rev Pharmacol Toxicol, 41, pp. 443-470
OSIRIS Property Explorer, Actelion Pharmaceuticals Ltd, Gewerbestrasse 16, 4123 Allschwil, , http://www.actelion.com/uninet/www/www_main_p.nsf/Content/Technologies+Property+Explorer, Switzerland. Available from
XLOGP, Molecular Design Laboratory, Institute of Physical Chemistry, Peking University, Beijing, China. Available from: ftp2.ipc.pku.edu.cn/pub/ software/xlogp/Reed, J.E., Woo, L.W.L., Robinson, J.J., 2-Difluoromethyloestrone 3-O-sulphamate, a highly potent steroid sulphatase inhibitor (2004) Biochem Biophys Res Commun, 317 (16), pp. 9-75
Woo, L.W.L., Bubert, C., Sutcliffe, O.B., Dual aromatase-steroid sulfatase inhibitors (2007) J Med Chem, 50, pp. 3540-3560
Howard, J.A.K., Hoy, V.J., O'Hagan, D., Smith, G.T., How good is fluorine as a hydrogen bond acceptor? (1996) Tetrahedron, 52, pp. 12613-12622
O'Hagen, D., Rzepa, H.S., Some influences of fluorine in bioorganic chemistry Chem Commun1997
Barbarich, T.J., Rithner, C.D., Miller, S.M., Anderson, O.P., Strauss, S.H., Significant inter- and intramolecular O-H⋯·F-C hydrogen bonding (1999) J Am Chem Soc, 121, pp. 4280-4281
Bohm, H.J., Banner, D., Bendels, S., Fluorine in medicinal chemistry (2004) ChemBioChem, 5, pp. 637-643
Shah, P., Westwell, A.D., The role of fluorine in medicinal chemistry (2007) J Enzyme Inhib Med Chem, 22, pp. 527-540
Poirier, D., Boivin, R.P., 17α-Alkyl- or 17α-substituted benzyl-17β-estradiols: A new family of estrone-sulfatase inhibitors (1998) Bioorg Med Chem Lett, 8, pp. 1891-1896
Boivin, R.P., Luu-The, V., Lachance, R., Labrie, F., Poirier, D., Structure-activity relationships of 17α-derivatives of estradiol as inhibitors of steroid sulfatase (2000) J Med Chem, 43, pp. 4465-4478
Woo, L.W.L., Howarth, N.M., Purohit, A., Hejaz, H.A., Reed, M.J., Potter, B.V.L., Steroidal and nonsteroidal sulfamates as potent inhibitors of steroid sulfatase (1998) J Med Chem, 41, pp. 1068-1083
Woo, L.W.L., Purohit, A., Malini, B., Reed, M.J., Potter, B.V.L., Potent active site-directed inhibition of steroid sulphatase by tricyclic coumarin-based sulphamates (2000) Chem Biol, 7, pp. 773-791
Chander, S.K., Purohit, A., Woo, L.W.L., Potter, B.V.L., Reed, M.J., The role of steroid sulphatase in regulating the oestrogenicity of oestrogen sulphamates (2004) Biochem Biophys Res Commun, 322, pp. 217-222
Ho, Y.T., Purohit, A., Vicker, N., Inhibition of carbonic anhydrase II by steroidal and non-steroidal sulphamates (2003) Biochem Biophys Res Commun, 305, pp. 909-914
Vicker, N., Ho, Y., Robinson, J., Docking studies of sulphamate inhibitors of estrone sulphatase in human carbonic anhydrase II (2003) Bioorg Med Chem Lett, 13, pp. 863-865
Leese, M.P., Leblond, B., Smith, A., 2-Substituted estradiol bis-sulfamates, multitargeted antitumor agents: Synthesis, in vitro SAR, protein crystallography, and in vivo activity (2006) J Med Chem, 49, pp. 7683-7696
Ireson, C.R., Chander, S.K., Purohit, A., Pharmacokinetics of the nonsteroidal steroid sulphatase inhibitor 667 COUMATE and its sequestration into red blood cells in rats (2004) Br J Cancer, 91, pp. 1399-1404
Abbate, F., Winum, J.Y., Potter, B.V.L., Carbonic anhydrase inhibitors: X-ray crystallographic structure of the adduct of human isozyme II with EMATE, a dual inhibitor of carbonic anhydrases and steroid sulfatase (2004) Bioorg Med Chem Lett, 14, pp. 231-234
Lloyd, M.D., Pederick, R.L., Natesh, R., Crystal structure of human carbonic anhydrase II at 1.95 A resolution in complex with 667-coumate, a novel anti-cancer agent (2005) Biochem J, 385, pp. 715-720
Lloyd, M.D., Thiyagarajan, N., Ho, Y.T., First crystal structures of human carbonic anhydrase II in complex with dual aromatase-steroid sulfatase inhibitors (2005) Biochemistry, 44, pp. 6858-6866
Leese, M.P., Jourdan, F., Gaukroger, K., Structure-activity relationships of C-17 cyanated estratrienes as anti-cancer agents (2008) J Med Chem, 51, pp. 1295-1308
Reed, M. J., Purohit, A., Woo, L. W. L., Newman, S. P., Potter, B. V. L., Steroid sulfatase: Molecular biology, regulation, and inhibition (2005) Endocr Rev, 26, pp. 171-20
Stanway, S. J., Purohit, A., Woo, L. W. L., Phase I study of STX 64 (667 Coumate) in breast cancer patients: The first study of a steroid sulfatase inhibitor (2006) Clin Cancer Res, 12, pp. 1585-1592
Foster, P. A., Newman, S. P., Chander, S. K., In vivo efficacy of STX213, a second-generation steroid sulfatase inhibitor, for hormone-dependent breast cancer therapy (2006) Clin Cancer Res, 12, pp. 5543-5549
Foster, P. A., Chander, S. K., Parsons, M. F., Efficacy of three potent steroid sulfatase inhibitors: Pre-clinical investigations for their use in the treatment of hormone-dependent breast cancer (2008) Breast Cancer Res Treat, 111, pp. 129-138
Stanway, S. J., Delavault, P., Purohit, A., Steroid sulfatase: A new target for the endocrine therapy of breast cancer (2007) Oncologist, 12, pp. 370-374
Fischer, D. S., Woo, L. W. L., Mahon, M. F., Purohit, A., Reed, M. J., Potter, B. V. L., D-ring modified estrone derivatives as novel potent inhibitors of steroid sulfatase (2003) Bioorg Med Chem, 11, pp. 1685-1700
Fischer, D. S., Chander, S. K., Woo, L. W. L., Novel D-ring modified steroid derivatives as potent, non-estrogenic, steroid sulfatase inhibitors with in vivo activity (2003) J Steroid Biochem Mol Biol, 84, pp. 343-349
57: 79-88Jones, G., Willett, P., Glen, R. C., Leach, A. R., Taylor, R., Development and validation of a genetic algorithm for flexible docking (1997) J Mol Biol, 267, pp. 727-748
Eriksson, A. E., Jones, T. A., Liljas, A., Refined structure of human carbonic anhydrase II at 2. 0 A resolution (1988) Proteins, 4, pp. 274-282
Brunger, A. T., Adams, P. D., Clore, G. M., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr D Biol Crystallogr, 54, pp. 905-921
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr A, 47, pp. 110-119
Laskowski, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M., PROCHECK - a program to check the stereochemical quality of protein structures (1993) J Appl Crystallogr, 26, pp. 283-291
Park, B. K., Kitteringham, N. R., O'Neill, P. M., Metabolism of fluorine-containing drugs (2001) Annu Rev Pharmacol Toxicol, 41, pp. 443-470
Woo, L. W. L., Bubert, C., Sutcliffe, O. B., Dual aromatase-steroid sulfatase inhibitors (2007) J Med Chem, 50, pp. 3540-3560
Howard, J. A. K., Hoy, V. J., O'Hagan, D., Smith, G. T., How good is fluorine as a hydrogen bond acceptor? (1996) Tetrahedron, 52, pp. 12613-12622
Barbarich, T. J., Rithner, C. D., Miller, S. M., Anderson, O. P., Strauss, S. H., Significant inter- and intramolecular O-H F-C hydrogen bonding (1999) J Am Chem Soc, 121, pp. 4280-4281
Bohm, H. J., Banner, D., Bendels, S., Fluorine in medicinal chemistry (2004) ChemBioChem, 5, pp. 637-643
Boivin, R. P., Luu-The, V., Lachance, R., Labrie, F., Poirier, D., Structure-activity relationships of 17 -derivatives of estradiol as inhibitors of steroid sulfatase (2000) J Med Chem, 43, pp. 4465-4478
Woo, L. W. L., Howarth, N. M., Purohit, A., Hejaz, H. A., Reed, M. J., Potter, B. V. L., Steroidal and nonsteroidal sulfamates as potent inhibitors of steroid sulfatase (1998) J Med Chem, 41, pp. 1068-1083
Woo, L. W. L., Purohit, A., Malini, B., Reed, M. J., Potter, B. V. L., Potent active site-directed inhibition of steroid sulphatase by tricyclic coumarin-based sulphamates (2000) Chem Biol, 7, pp. 773-791
Chander, S. K., Purohit, A., Woo, L. W. L., Potter, B. V. L., Reed, M. J., The role of steroid sulphatase in regulating the oestrogenicity of oestrogen sulphamates (2004) Biochem Biophys Res Commun, 322, pp. 217-222
Ho, Y. T., Purohit, A., Vicker, N., Inhibition of carbonic anhydrase II by steroidal and non-steroidal sulphamates (2003) Biochem Biophys Res Commun, 305, pp. 909-914
Leese, M. P., Leblond, B., Smith, A., 2-Substituted estradiol bis-sulfamates, multitargeted antitumor agents: Synthesis, in vitro SAR, protein crystallography, and in vivo activity (2006) J Med Chem, 49, pp. 7683-7696
Ireson, C. R., Chander, S. K., Purohit, A., Pharmacokinetics of the nonsteroidal steroid sulphatase inhibitor 667 COUMATE and its sequestration into red blood cells in rats (2004) Br J Cancer, 91, pp. 1399-1404
Lloyd, M. D., Pederick, R. L., Natesh, R., Crystal structure of human carbonic anhydrase II at 1. 95 A resolution in complex with 667-coumate, a novel anti-cancer agent (2005) Biochem J, 385, pp. 715-720
Lloyd, M. D., Thiyagarajan, N., Ho, Y. T., First crystal structures of human carbonic anhydrase II in complex with dual aromatase-steroid sulfatase inhibitors (2005) Biochemistry, 44, pp. 6858-6866
Leese, M. P., Jourdan, F., Gaukroger, K., Structure-activity relationships of C-17 cyanated estratrienes as anti-cancer agents (2008) J Med Chem, 51, pp. 1295-1308
Mol Cancer Ther (ISSN: 1535-7163, 1538-8514electronic), 2008 Sep; 7(8): 2435-2444.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.003, 5-year impact factor: 5.428
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-53349089862&partnerID=40&md5=4d4f3c49bf6a556109d89d26b4e5ea48
Keywords: 3 Hydroxy N 3, 3 Trifluoropropyl 16, 17 Seco Estra 1, 5(10) Triene 16, 17 Imide, 3 Sulfamoyloxy N 3, 667 Coumarin, Antineoplastic Agent, Estrone, Estrone 3 O Sulfamic Acid, Stx 64, Unclassified Drug, Animal Experiment, Animal Model, Antineoplastic Activity, Article, Binding Site, Breast Cancer, Controlled Study, Crystallization, Crystallography, Drug Synthesis, Female, Hydrogen Bond, Hydrophobicity, Molecular Model, Nonhuman, Priority Journal, Protein Interaction, Single Drug Dose, Chromatography, Liquid, X-Ray, Enzyme Inhibitors, Fluorine, Magnetic Resonance Spectroscopy, Protein Conformation, Wistar, Spectrometry, Electrospray Ionization, Steryl-Sulfatase, 5 (10) Triene 16,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy and Pharmacology, Sterix Ltd., University of Bath, Bath, United Kingdom
Department of Endocrinology and Metabolic Medicine, Imperial College London, St. Mary's Hospital, London, United Kingdom
Istituto di Biostrutture e Bioimmagini-CNR, Naples, Italy
Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Florence, Italy
Universit degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Florence, Italy
References:
Reed, M.J., Purohit, A., Woo, L.W.L., Newman, S.P., Potter, B.V.L., Steroid sulfatase: Molecular biology, regulation, and inhibition (2005) Endocr Rev, 26, pp. 171-20
Stanway, S.J., Purohit, A., Woo, L.W.L., Phase I study of STX 64 (667 Coumate) in breast cancer patients: The first study of a steroid sulfatase inhibitor (2006) Clin Cancer Res, 12, pp. 1585-1592
Elger, W., Schwarz, S., Hedden, A., Reddersen, G., Schneider, B., Sulfamates of various estrogens are prodrugs with increased systemic and reduced hepatic estrogenicity at oral application (1995) J Steroid Biochem Mol Biol, 55, pp. 395-403
Foster, P.A., Newman, S.P., Chander, S.K., In vivo efficacy of STX213, a second-generation steroid sulfatase inhibitor, for hormone-dependent breast cancer therapy (2006) Clin Cancer Res, 12, pp. 5543-5549
Foster, P.A., Chander, S.K., Parsons, M.F., Efficacy of three potent steroid sulfatase inhibitors: Pre-clinical investigations for their use in the treatment of hormone-dependent breast cancer (2008) Breast Cancer Res Treat, 111, pp. 129-138
Stanway, S.J., Delavault, P., Purohit, A., Steroid sulfatase: A new target for the endocrine therapy of breast cancer (2007) Oncologist, 12, pp. 370-374
Fischer, D.S., Woo, L.W.L., Mahon, M.F., Purohit, A., Reed, M.J., Potter, B.V.L., D-ring modified estrone derivatives as novel potent inhibitors of steroid sulfatase (2003) Bioorg Med Chem, 11, pp. 1685-1700
Fischer, D.S., Chander, S.K., Woo, L.W.L., Novel D-ring modified steroid derivatives as potent, non-estrogenic, steroid sulfatase inhibitors with in vivo activity (2003) J Steroid Biochem Mol Biol, 84, pp. 343-349
Purohit, A., Williams, G.J., Roberts, C.J., Potter, B.V.L., Reed, M.J., In vivo inhibition of oestrone sulphatase and dehydroepiandrosterone sulphatase by oestrone-3-O-sulphamate (1995) Int J Cancer, 63, pp. 106-111
Hernandez-Guzman, F.G., Higashiyama, T., Pangborn, W., Osawa, Y., Ghosh, D., Structure of human estrone sulfatase suggests functional roles of membrane association (2003) J Biol Chem, 278, pp. 22989-22997
Woo LWL, Lightowler M, Purohit A, Reed MJ, Potter BVL. Heteroatom-substituted analogues of the active-site directed inhibitor estra-1,3,5(10)-trien-17-one-3-sulphamate inhibit estrone sulphatase by a different mechanism. J Steroid Biochem Mol Biol 1996
57:79-88Jones, G., Willett, P., Glen, R.C., Leach, A.R., Taylor, R., Development and validation of a genetic algorithm for flexible docking (1997) J Mol Biol, 267, pp. 727-748
Eriksson, A.E., Jones, T.A., Liljas, A., Refined structure of human carbonic anhydrase II at 2.0 A resolution (1988) Proteins, 4, pp. 274-282
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol, 276, pp. 307-326
Brunger, A.T., Adams, P.D., Clore, G.M., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr D Biol Crystallogr, 54, pp. 905-921
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr A, 47, pp. 110-119
Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK - a program to check the stereochemical quality of protein structures (1993) J Appl Crystallogr, 26, pp. 283-291
Park, B.K., Kitteringham, N.R., O'Neill, P.M., Metabolism of fluorine-containing drugs (2001) Annu Rev Pharmacol Toxicol, 41, pp. 443-470
OSIRIS Property Explorer, Actelion Pharmaceuticals Ltd, Gewerbestrasse 16, 4123 Allschwil, , http://www.actelion.com/uninet/www/www_main_p.nsf/Content/Technologies+Property+Explorer, Switzerland. Available from
XLOGP, Molecular Design Laboratory, Institute of Physical Chemistry, Peking University, Beijing, China. Available from: ftp2.ipc.pku.edu.cn/pub/ software/xlogp/Reed, J.E., Woo, L.W.L., Robinson, J.J., 2-Difluoromethyloestrone 3-O-sulphamate, a highly potent steroid sulphatase inhibitor (2004) Biochem Biophys Res Commun, 317 (16), pp. 9-75
Woo, L.W.L., Bubert, C., Sutcliffe, O.B., Dual aromatase-steroid sulfatase inhibitors (2007) J Med Chem, 50, pp. 3540-3560
Howard, J.A.K., Hoy, V.J., O'Hagan, D., Smith, G.T., How good is fluorine as a hydrogen bond acceptor? (1996) Tetrahedron, 52, pp. 12613-12622
O'Hagen, D., Rzepa, H.S., Some influences of fluorine in bioorganic chemistry Chem Commun1997
Barbarich, T.J., Rithner, C.D., Miller, S.M., Anderson, O.P., Strauss, S.H., Significant inter- and intramolecular O-H⋯·F-C hydrogen bonding (1999) J Am Chem Soc, 121, pp. 4280-4281
Bohm, H.J., Banner, D., Bendels, S., Fluorine in medicinal chemistry (2004) ChemBioChem, 5, pp. 637-643
Shah, P., Westwell, A.D., The role of fluorine in medicinal chemistry (2007) J Enzyme Inhib Med Chem, 22, pp. 527-540
Poirier, D., Boivin, R.P., 17α-Alkyl- or 17α-substituted benzyl-17β-estradiols: A new family of estrone-sulfatase inhibitors (1998) Bioorg Med Chem Lett, 8, pp. 1891-1896
Boivin, R.P., Luu-The, V., Lachance, R., Labrie, F., Poirier, D., Structure-activity relationships of 17α-derivatives of estradiol as inhibitors of steroid sulfatase (2000) J Med Chem, 43, pp. 4465-4478
Woo, L.W.L., Howarth, N.M., Purohit, A., Hejaz, H.A., Reed, M.J., Potter, B.V.L., Steroidal and nonsteroidal sulfamates as potent inhibitors of steroid sulfatase (1998) J Med Chem, 41, pp. 1068-1083
Woo, L.W.L., Purohit, A., Malini, B., Reed, M.J., Potter, B.V.L., Potent active site-directed inhibition of steroid sulphatase by tricyclic coumarin-based sulphamates (2000) Chem Biol, 7, pp. 773-791
Chander, S.K., Purohit, A., Woo, L.W.L., Potter, B.V.L., Reed, M.J., The role of steroid sulphatase in regulating the oestrogenicity of oestrogen sulphamates (2004) Biochem Biophys Res Commun, 322, pp. 217-222
Ho, Y.T., Purohit, A., Vicker, N., Inhibition of carbonic anhydrase II by steroidal and non-steroidal sulphamates (2003) Biochem Biophys Res Commun, 305, pp. 909-914
Vicker, N., Ho, Y., Robinson, J., Docking studies of sulphamate inhibitors of estrone sulphatase in human carbonic anhydrase II (2003) Bioorg Med Chem Lett, 13, pp. 863-865
Leese, M.P., Leblond, B., Smith, A., 2-Substituted estradiol bis-sulfamates, multitargeted antitumor agents: Synthesis, in vitro SAR, protein crystallography, and in vivo activity (2006) J Med Chem, 49, pp. 7683-7696
Ireson, C.R., Chander, S.K., Purohit, A., Pharmacokinetics of the nonsteroidal steroid sulphatase inhibitor 667 COUMATE and its sequestration into red blood cells in rats (2004) Br J Cancer, 91, pp. 1399-1404
Abbate, F., Winum, J.Y., Potter, B.V.L., Carbonic anhydrase inhibitors: X-ray crystallographic structure of the adduct of human isozyme II with EMATE, a dual inhibitor of carbonic anhydrases and steroid sulfatase (2004) Bioorg Med Chem Lett, 14, pp. 231-234
Lloyd, M.D., Pederick, R.L., Natesh, R., Crystal structure of human carbonic anhydrase II at 1.95 A resolution in complex with 667-coumate, a novel anti-cancer agent (2005) Biochem J, 385, pp. 715-720
Lloyd, M.D., Thiyagarajan, N., Ho, Y.T., First crystal structures of human carbonic anhydrase II in complex with dual aromatase-steroid sulfatase inhibitors (2005) Biochemistry, 44, pp. 6858-6866
Leese, M.P., Jourdan, F., Gaukroger, K., Structure-activity relationships of C-17 cyanated estratrienes as anti-cancer agents (2008) J Med Chem, 51, pp. 1295-1308
Reed, M. J., Purohit, A., Woo, L. W. L., Newman, S. P., Potter, B. V. L., Steroid sulfatase: Molecular biology, regulation, and inhibition (2005) Endocr Rev, 26, pp. 171-20
Stanway, S. J., Purohit, A., Woo, L. W. L., Phase I study of STX 64 (667 Coumate) in breast cancer patients: The first study of a steroid sulfatase inhibitor (2006) Clin Cancer Res, 12, pp. 1585-1592
Foster, P. A., Newman, S. P., Chander, S. K., In vivo efficacy of STX213, a second-generation steroid sulfatase inhibitor, for hormone-dependent breast cancer therapy (2006) Clin Cancer Res, 12, pp. 5543-5549
Foster, P. A., Chander, S. K., Parsons, M. F., Efficacy of three potent steroid sulfatase inhibitors: Pre-clinical investigations for their use in the treatment of hormone-dependent breast cancer (2008) Breast Cancer Res Treat, 111, pp. 129-138
Stanway, S. J., Delavault, P., Purohit, A., Steroid sulfatase: A new target for the endocrine therapy of breast cancer (2007) Oncologist, 12, pp. 370-374
Fischer, D. S., Woo, L. W. L., Mahon, M. F., Purohit, A., Reed, M. J., Potter, B. V. L., D-ring modified estrone derivatives as novel potent inhibitors of steroid sulfatase (2003) Bioorg Med Chem, 11, pp. 1685-1700
Fischer, D. S., Chander, S. K., Woo, L. W. L., Novel D-ring modified steroid derivatives as potent, non-estrogenic, steroid sulfatase inhibitors with in vivo activity (2003) J Steroid Biochem Mol Biol, 84, pp. 343-349
57: 79-88Jones, G., Willett, P., Glen, R. C., Leach, A. R., Taylor, R., Development and validation of a genetic algorithm for flexible docking (1997) J Mol Biol, 267, pp. 727-748
Eriksson, A. E., Jones, T. A., Liljas, A., Refined structure of human carbonic anhydrase II at 2. 0 A resolution (1988) Proteins, 4, pp. 274-282
Brunger, A. T., Adams, P. D., Clore, G. M., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr D Biol Crystallogr, 54, pp. 905-921
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr A, 47, pp. 110-119
Laskowski, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M., PROCHECK - a program to check the stereochemical quality of protein structures (1993) J Appl Crystallogr, 26, pp. 283-291
Park, B. K., Kitteringham, N. R., O'Neill, P. M., Metabolism of fluorine-containing drugs (2001) Annu Rev Pharmacol Toxicol, 41, pp. 443-470
Woo, L. W. L., Bubert, C., Sutcliffe, O. B., Dual aromatase-steroid sulfatase inhibitors (2007) J Med Chem, 50, pp. 3540-3560
Howard, J. A. K., Hoy, V. J., O'Hagan, D., Smith, G. T., How good is fluorine as a hydrogen bond acceptor? (1996) Tetrahedron, 52, pp. 12613-12622
Barbarich, T. J., Rithner, C. D., Miller, S. M., Anderson, O. P., Strauss, S. H., Significant inter- and intramolecular O-H F-C hydrogen bonding (1999) J Am Chem Soc, 121, pp. 4280-4281
Bohm, H. J., Banner, D., Bendels, S., Fluorine in medicinal chemistry (2004) ChemBioChem, 5, pp. 637-643
Boivin, R. P., Luu-The, V., Lachance, R., Labrie, F., Poirier, D., Structure-activity relationships of 17 -derivatives of estradiol as inhibitors of steroid sulfatase (2000) J Med Chem, 43, pp. 4465-4478
Woo, L. W. L., Howarth, N. M., Purohit, A., Hejaz, H. A., Reed, M. J., Potter, B. V. L., Steroidal and nonsteroidal sulfamates as potent inhibitors of steroid sulfatase (1998) J Med Chem, 41, pp. 1068-1083
Woo, L. W. L., Purohit, A., Malini, B., Reed, M. J., Potter, B. V. L., Potent active site-directed inhibition of steroid sulphatase by tricyclic coumarin-based sulphamates (2000) Chem Biol, 7, pp. 773-791
Chander, S. K., Purohit, A., Woo, L. W. L., Potter, B. V. L., Reed, M. J., The role of steroid sulphatase in regulating the oestrogenicity of oestrogen sulphamates (2004) Biochem Biophys Res Commun, 322, pp. 217-222
Ho, Y. T., Purohit, A., Vicker, N., Inhibition of carbonic anhydrase II by steroidal and non-steroidal sulphamates (2003) Biochem Biophys Res Commun, 305, pp. 909-914
Leese, M. P., Leblond, B., Smith, A., 2-Substituted estradiol bis-sulfamates, multitargeted antitumor agents: Synthesis, in vitro SAR, protein crystallography, and in vivo activity (2006) J Med Chem, 49, pp. 7683-7696
Ireson, C. R., Chander, S. K., Purohit, A., Pharmacokinetics of the nonsteroidal steroid sulphatase inhibitor 667 COUMATE and its sequestration into red blood cells in rats (2004) Br J Cancer, 91, pp. 1399-1404
Lloyd, M. D., Pederick, R. L., Natesh, R., Crystal structure of human carbonic anhydrase II at 1. 95 A resolution in complex with 667-coumate, a novel anti-cancer agent (2005) Biochem J, 385, pp. 715-720
Lloyd, M. D., Thiyagarajan, N., Ho, Y. T., First crystal structures of human carbonic anhydrase II in complex with dual aromatase-steroid sulfatase inhibitors (2005) Biochemistry, 44, pp. 6858-6866
Leese, M. P., Jourdan, F., Gaukroger, K., Structure-activity relationships of C-17 cyanated estratrienes as anti-cancer agents (2008) J Med Chem, 51, pp. 1295-1308
Anticancer steroid sulfatase inhibitors: synthesis of a potent fluorinated second-generation agent, in vitro and in vivo activities, molecular modeling, and protein crystallography
An improved steroid sulfatase inhibitor was prepared by replacing the N-propyl group of the second-generation steroid-like inhibitor (2) with a N-3,3,3-trifluoropropyl group to give (10). This compound is 5-fold more potent in vitro, completely inhibits rat liver steroid sulfatase activity after a single oral dose of 0.5 mg/kg, and exhibits a significantly longer duration of inhibition over (2). These biological properties are attributed to the increased lipophilicity and metabolic stability of (10) rendered by its trifluoropropyl group and also the potential H-bonding between its fluorine atom(s) and Arg 98 in the active site of human steroid sulfatase. Like other sulfamates, (10) is expected to be sequestered, and transported by, erythrocytes in vivo because it inhibits human carbonic anhydrase II (hCAII) potently (IC50, 3 nmol/L). A congener (4), which possesses a N-(pyridin-3-ylmethyl) substituent, is even more active (IC50, 0.1 nmol/L). To rationalize this, the hCAII-(4) adduct, obtained by cocrystallization, reveals not only the sulfamate group and the backbone of (4) interacting with the catalytic site and the associated hydrophobic pocket, respectively, but also the potential H-bonding between the N-(pyridin-3- ylmethyl) group and Nε2 of Gln136. Like (2), both (10) and its phenolic precursor (9) are non-estrogenic using a uterine weight gain assay. In summary, a highly potent, long-acting, and nonestrogenic steroid sulfatase inhibitor was designed with hCAII inhibitory properties that should positively influence in vivo behavior. Compound (10) and other related inhibitors of this structural class further expand the armory of steroid sulfatase inhibitors against hormone-dependent breast cancer. Copyright © 2008 American Association for Cancer Research.
An improved steroid sulfatase inhibitor was prepared by replacing the N-propyl group of the second-generation steroid-like inhibitor (2) with a N-3,3,3-trifluoropropyl group to give (10). This compound is 5-fold more potent in vitro, completely inhibits rat liver steroid sulfatase activity after a single oral dose of 0.5 mg/kg, and exhibits a significantly longer duration of inhibition over (2). These biological properties are attributed to the increased lipophilicity and metabolic stability of (10) rendered by its trifluoropropyl group and also the potential H-bonding between its fluorine atom(s) and Arg 98 in the active site of human steroid sulfatase. Like other sulfamates, (10) is expected to be sequestered, and transported by, erythrocytes in vivo because it inhibits human carbonic anhydrase II (hCAII) potently (IC50, 3 nmol/L). A congener (4), which possesses a N-(pyridin-3-ylmethyl) substituent, is even more active (IC50, 0.1 nmol/L). To rationalize this, the hCAII-(4) adduct, obtained by cocrystallization, reveals not only the sulfamate group and the backbone of (4) interacting with the catalytic site and the associated hydrophobic pocket, respectively, but also the potential H-bonding between the N-(pyridin-3- ylmethyl) group and Nε2 of Gln136. Like (2), both (10) and its phenolic precursor (9) are non-estrogenic using a uterine weight gain assay. In summary, a highly potent, long-acting, and nonestrogenic steroid sulfatase inhibitor was designed with hCAII inhibitory properties that should positively influence in vivo behavior. Compound (10) and other related inhibitors of this structural class further expand the armory of steroid sulfatase inhibitors against hormone-dependent breast cancer. Copyright © 2008 American Association for Cancer Research.
Anticancer steroid sulfatase inhibitors: synthesis of a potent fluorinated second-generation agent, in vitro and in vivo activities, molecular modeling, and protein crystallography
No results. |
644 views. Last view on Sunday 12 March 2023, 19:49:47
ibb.cnr.it
