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Volumn 46, Issue 26, 2003, Pages 5619-5627

Rational Design of an Indolebutanoic Acid Derivative as a Novel Aldose Reductase Inhibitor Based on Docking and 3D QSAR Studies of Phenethylamine Derivatives

Author keywords

[No Author keywords available]

Indexed keywords

4 OXO 4 (4 HYDROXYINDOLE)BUTANOIC ACID; ALDEHYDE REDUCTASE; ALDOSE REDUCTASE INHIBITOR; BUTYRIC ACID DERIVATIVE; INDOLEBUTANOIC ACID DERIVATIVE; N 2 METHYLBUTANOYLTYRAMINE; PHENETHYLAMINE DERIVATIVE; TOLRESTAT; UNCLASSIFIED DRUG; YUA 001;

EID: 0347627163     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm0205346     Document Type: Article
Times cited : (34)

References (47)
  • 1
    • 0028859525 scopus 로고
    • Clinical trials of diabetic neuropathy: Past, present, and future
    • Pfeifer, M. A.; Schumer, M. P. Clinical trials of diabetic neuropathy: Past, present, and future. Diabetes 1995, 44, 1355-1361.
    • (1995) Diabetes , vol.44 , pp. 1355-1361
    • Pfeifer, M.A.1    Schumer, M.P.2
  • 2
    • 0025267721 scopus 로고
    • Glucose-induced microvascular functional changes in nondiabetic rats are stereospecific and are prevented by an aldose reductase inhibitor
    • Williamson, J. R.; Ostrow, E.; Eades, D.; Chang, K.; Allison, W.; Kilo, C.; Sherman, W. R. Glucose-induced microvascular functional changes in nondiabetic rats are stereospecific and are prevented by an aldose reductase inhibitor. J. Clin. Invest. 1990, 85, 1167-1172.
    • (1990) J. Clin. Invest. , vol.85 , pp. 1167-1172
    • Williamson, J.R.1    Ostrow, E.2    Eades, D.3    Chang, K.4    Allison, W.5    Kilo, C.6    Sherman, W.R.7
  • 3
    • 0021203809 scopus 로고
    • Human placenta aldose reductase: Forms sensitive and insensitive to inhibition by alrestatin
    • Maragoudakis, M. E.; Wasvary, J.; Hankin, H.; Gargiulo, P. Human placenta aldose reductase: Forms sensitive and insensitive to inhibition by alrestatin. Mol. Pharmacol. 1984, 25, 425-430.
    • (1984) Mol. Pharmacol. , vol.25 , pp. 425-430
    • Maragoudakis, M.E.1    Wasvary, J.2    Hankin, H.3    Gargiulo, P.4
  • 4
    • 0031058373 scopus 로고    scopus 로고
    • Highly selective aldose reductase inhibitors. 3. Structural diversity of 3-(arylmethyl)-2,4,5-trioxoimidazolidine-1-acetic acids
    • Kotani, T.; Nagaki, Y.; Ishii, A.; Konishi, Y.; Yaho, H.; Suehiro, S.; Okukado, N.; Okamoto, K. Highly selective aldose reductase inhibitors. 3. Structural diversity of 3-(arylmethyl)-2,4,5-trioxoimidazolidine-1-acetic acids. J. Med. Chem. 1997, 40, 684-694.
    • (1997) J. Med. Chem. , vol.40 , pp. 684-694
    • Kotani, T.1    Nagaki, Y.2    Ishii, A.3    Konishi, Y.4    Yaho, H.5    Suehiro, S.6    Okukado, N.7    Okamoto, K.8
  • 6
    • 0035902432 scopus 로고    scopus 로고
    • Stereospecific interaction of a novel spirosuccinimide type aldose reductase inhibitor, AS-3201, with aldose reductase
    • Kurono, M.; Fujiwara, I.; Yoshida, K. Stereospecific interaction of a novel spirosuccinimide type aldose reductase inhibitor, AS-3201, with aldose reductase. Biochemistry 2001, 40, 8216-8226.
    • (2001) Biochemistry , vol.40 , pp. 8216-8226
    • Kurono, M.1    Fujiwara, I.2    Yoshida, K.3
  • 7
    • 0001367596 scopus 로고    scopus 로고
    • Development of Eparlestat (Kinedak), aldose reductase inhibitor
    • Kawamura, M.; Hamanaka, N. Development of Eparlestat (Kinedak), aldose reductase inhibitor. J. Synth. Org. Chem. 1997, 37, 787-792.
    • (1997) J. Synth. Org. Chem. , vol.37 , pp. 787-792
    • Kawamura, M.1    Hamanaka, N.2
  • 9
    • 0032548075 scopus 로고    scopus 로고
    • Synthesis, activity, and molecular modeling of new 2,4-dioxo-5-(naphthylene)-3-thiazolidineacetic acids and 2-thioxo analogues as potent aldose reductase inhibitors
    • Fresneau, P.; Cussac, M.; Morand, J. M.; Szymonski, B.; Tranqui, D.; Leclerc, G. Synthesis, activity, and molecular modeling of new 2,4-dioxo-5-(naphthylene)-3-thiazolidineacetic acids and 2-thioxo analogues as potent aldose reductase inhibitors. J. Med. Chem. 1998, 41, 4706-4715.
    • (1998) J. Med. Chem. , vol.41 , pp. 4706-4715
    • Fresneau, P.1    Cussac, M.2    Morand, J.M.3    Szymonski, B.4    Tranqui, D.5    Leclerc, G.6
  • 10
    • 0031424157 scopus 로고    scopus 로고
    • The alrestatin double-decker: Binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant
    • Harrison, D. H.; Bohren, K. M.; Petsko, G. A.; Ringe, D.; Gabbay, K. H. The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant. Biochemistry 1997, 36, 16134-16140.
    • (1997) Biochemistry , vol.36 , pp. 16134-16140
    • Harrison, D.H.1    Bohren, K.M.2    Petsko, G.A.3    Ringe, D.4    Gabbay, K.H.5
  • 11
    • 0031920049 scopus 로고    scopus 로고
    • Aldose reductase in glucose toxicity: A potential target for the prevention of diabetic complications
    • Yabe-Nishimura, C. Aldose reductase in glucose toxicity: A potential target for the prevention of diabetic complications. Pharmacol. Rev. 1998, 50, 21-33.
    • (1998) Pharmacol. Rev. , vol.50 , pp. 21-33
    • Yabe-Nishimura, C.1
  • 12
    • 0030982582 scopus 로고    scopus 로고
    • Studies on the inhibitor-binding site of porcine aldehyde reductase: Crystal structure of the holoenzyme-inhibitor ternary complex
    • El-Kabbani, O.; Carper, D. A.; McGowan, M. H.; Devedjiev, Y.; Rees-Milton, K. J.; Flynn, T. G. Studies on the inhibitor-binding site of porcine aldehyde reductase: Crystal structure of the holoenzyme-inhibitor ternary complex. Proteins 1997, 29, 186-192.
    • (1997) Proteins , vol.29 , pp. 186-192
    • El-Kabbani, O.1    Carper, D.A.2    McGowan, M.H.3    Devedjiev, Y.4    Rees-Milton, K.J.5    Flynn, T.G.6
  • 13
    • 0029756487 scopus 로고    scopus 로고
    • Kinetic and spectroscopic evidence for active site inhibition of human aldose reductase
    • Nakano, T.; Petrash, J. M. Kinetic and spectroscopic evidence for active site inhibition of human aldose reductase. Biochemistry 1996, 35, 11196-11202.
    • (1996) Biochemistry , vol.35 , pp. 11196-11202
    • Nakano, T.1    Petrash, J.M.2
  • 14
    • 0038167343 scopus 로고    scopus 로고
    • Computer simulation studies of the catalytic mechanism of human aldose reductase
    • Varnai, P.; Warshel, A. Computer simulation studies of the catalytic mechanism of human aldose reductase. J. Am. Chem. Soc. 2000, 122, 3849-3860.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3849-3860
    • Varnai, P.1    Warshel, A.2
  • 16
    • 0034704811 scopus 로고    scopus 로고
    • Molecular modeling of the aldose reductase-inhibitor complex based on the X-ray crystal structure and studies with single-site-directed mutants
    • Singh, S. B.; Malamas, M. S.; Hohman, T. C.; Nilakantan, R.; Carper, D. A.; Kitchen, D. Molecular modeling of the aldose reductase-inhibitor complex based on the X-ray crystal structure and studies with single-site-directed mutants. J. Med. Chem. 2000, 43, 1062-1070.
    • (2000) J. Med. Chem. , vol.43 , pp. 1062-1070
    • Singh, S.B.1    Malamas, M.S.2    Hohman, T.C.3    Nilakantan, R.4    Carper, D.A.5    Kitchen, D.6
  • 17
    • 0033915982 scopus 로고    scopus 로고
    • Recent advances in structure-based rational drug design
    • Gane, P. J.; Dean, P. M. Recent advances in structure-based rational drug design. Curr. Opin. Struct. Biol. 2000, 10, 401-404.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 401-404
    • Gane, P.J.1    Dean, P.M.2
  • 18
    • 0032828061 scopus 로고    scopus 로고
    • Computational approaches to structure-based ligand design
    • Joseph-McCarthy, D. Computational approaches to structure-based ligand design. Pharmacol. Ther. 1999, 84, 179-191.
    • (1999) Pharmacol. Ther. , vol.84 , pp. 179-191
    • Joseph-McCarthy, D.1
  • 19
    • 0035950118 scopus 로고    scopus 로고
    • Measuring Molecular Similarity and Diversity: Total Pharmacophore Diversity
    • Makara, G. M. Measuring Molecular Similarity and Diversity: Total Pharmacophore Diversity. J. Med. Chem. 2001, 44, 3563-3571.
    • (2001) J. Med. Chem. , vol.44 , pp. 3563-3571
    • Makara, G.M.1
  • 20
    • 0033545622 scopus 로고    scopus 로고
    • A general and fast scoring function for protein-ligand interactions: A simplified potential approach
    • Muegge, I.; Martin, Y. C. A general and fast scoring function for protein-ligand interactions: a simplified potential approach. J. Med. Chem. 1999, 42, 791-804.
    • (1999) J. Med. Chem. , vol.42 , pp. 791-804
    • Muegge, I.1    Martin, Y.C.2
  • 21
    • 0035966871 scopus 로고    scopus 로고
    • Detailed analysis of scoring function for virtual screening
    • Stahl, M.; Rarey, M. Detailed analysis of scoring function for virtual screening. J. Med. Chem. 2001, 44, 1035-1042.
    • (2001) J. Med. Chem. , vol.44 , pp. 1035-1042
    • Stahl, M.1    Rarey, M.2
  • 23
    • 0034581968 scopus 로고    scopus 로고
    • High-throughput and virtual screening: Core lead discovery technologies move towards integration
    • Good, A. C.; Krystek, S. R.; Mason, J. S. High-throughput and virtual screening: core lead discovery technologies move towards integration. Drug Discovery Today 2000, 5, 561-569.
    • (2000) Drug Discovery Today , vol.5 , pp. 561-569
    • Good, A.C.1    Krystek, S.R.2    Mason, J.S.3
  • 24
    • 0034649618 scopus 로고    scopus 로고
    • Protein-based virtual screening of chemical database. 1. Evaluation of different docking/scoring combinations
    • Bissantz, C.; Folkers, G.; Rognan, D. Protein-based virtual screening of chemical database. 1. Evaluation of different docking/scoring combinations. J. Med. Chem. 2000, 43, 4759-4767.
    • (2000) J. Med. Chem. , vol.43 , pp. 4759-4767
    • Bissantz, C.1    Folkers, G.2    Rognan, D.3
  • 25
    • 0035439436 scopus 로고    scopus 로고
    • 7-Hydroxy-2-substituted-4-H-1-benzopyran-4-one derivatives as aldose reductase inhibitors: A SAR study
    • Costantino, L.; Corso, A. D.; Rastelli, G.; Petrash, J. M.; Mura, U. 7-Hydroxy-2-substituted-4-H-1-benzopyran-4-one derivatives as aldose reductase inhibitors: a SAR study. Eur. J. Med. Chem. 2001, 36, 697-703.
    • (2001) Eur. J. Med. Chem. , vol.36 , pp. 697-703
    • Costantino, L.1    Corso, A.D.2    Rastelli, G.3    Petrash, J.M.4    Mura, U.5
  • 27
    • 0036191826 scopus 로고    scopus 로고
    • Discovery of new inhibitors of aldose reductase from molecular docking and database screening
    • Rastelli, G.; Ferrari, A. M.; Costantino, L.; Gamberini, M. C. Discovery of new inhibitors of aldose reductase from molecular docking and database screening. Bioorg. Med. Chem. 2002, 10, 1437-1450.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 1437-1450
    • Rastelli, G.1    Ferrari, A.M.2    Costantino, L.3    Gamberini, M.C.4
  • 28
    • 0035942512 scopus 로고    scopus 로고
    • Discovery of novel aldose reductase inhibitors using a protein structure-based approach: 3D-database search followed by design and synthesis
    • Iwata, Y.; Arisawa, M.; Hamada, R.; Kita, Y.; Mizutani, M. Y.; Tomioka, N.; Itai, A.; Miyamoto, S. Discovery of novel aldose reductase inhibitors using a protein structure-based approach: 3D-database search followed by design and synthesis. J. Med. Chem. 2001, 44, 1718-1728.
    • (2001) J. Med. Chem. , vol.44 , pp. 1718-1728
    • Iwata, Y.1    Arisawa, M.2    Hamada, R.3    Kita, Y.4    Mizutani, M.Y.5    Tomioka, N.6    Itai, A.7    Miyamoto, S.8
  • 29
    • 0031787051 scopus 로고    scopus 로고
    • YUA001, a novel aldose reductase inhibitor isolated from alkalophilic Corynebacterium sp. YUA25: I. Taxonomy, fermentation, isolation and characterization
    • Bahn, Y. S.; Park, J. M.; Bai, D. H.; Takase, S.; Yu, J. H. YUA001, a novel aldose reductase inhibitor isolated from alkalophilic Corynebacterium sp. YUA25: I. taxonomy, fermentation, isolation and characterization. J. Antibiotics 1998, 10, 902-907.
    • (1998) J. Antibiotics , vol.10 , pp. 902-907
    • Bahn, Y.S.1    Park, J.M.2    Bai, D.H.3    Takase, S.4    Yu, J.H.5
  • 30
    • 0035957528 scopus 로고    scopus 로고
    • FlexE: Efficient molecular docking considering protein structure variations
    • Claussen, H.; Buning, C.; Rarey, M.; Lengauer, T. FlexE: Efficient molecular docking considering protein structure variations. J. Mol. Biol. 2001, 308, 377-395.
    • (2001) J. Mol. Biol. , vol.308 , pp. 377-395
    • Claussen, H.1    Buning, C.2    Rarey, M.3    Lengauer, T.4
  • 31
    • 0034800971 scopus 로고    scopus 로고
    • The 3-D QSAR study of anticancer 1-N-substituted imidazo- and pyrrolo-quinoline-4,9-dione derivatives by CoMFA and CoMSIA
    • Suh, M. E.; Kang, M. J.; Park, S. Y. The 3-D QSAR study of anticancer 1-N-substituted imidazo- and pyrrolo-quinoline-4,9-dione derivatives by CoMFA and CoMSIA. Bioorg. Med. Chem. 2001, 9, 2987-2991.
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 2987-2991
    • Suh, M.E.1    Kang, M.J.2    Park, S.Y.3
  • 32
    • 0033757280 scopus 로고    scopus 로고
    • Linking CoMFA and protein homology models of enzyme-inhibitor interactions: An Application to nonsteroidal aromatase inhibitors
    • Cavalli, A.; Greco, G.; Novellino, E.; Recanatini, M. Linking CoMFA and protein homology models of enzyme-inhibitor interactions: an Application to nonsteroidal aromatase inhibitors. Bioorg. Med. Chem. 2000, 8, 2771-2780.
    • (2000) Bioorg. Med. Chem. , vol.8 , pp. 2771-2780
    • Cavalli, A.1    Greco, G.2    Novellino, E.3    Recanatini, M.4
  • 33
    • 0034597030 scopus 로고    scopus 로고
    • Computer-aided design, synthesis and biological assay of p-methylsulfonamido phenylethylamine analogues
    • Liu, H.; Ji, M.; Jiang, H.; Liu, L.; Hua, W.; Chen, K.; Ji, R. Computer-aided design, synthesis and biological assay of p-methylsulfonamido phenylethylamine analogues. Bioorg. Med. Chem. Lett. 2000, 10, 2153-2157.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 2153-2157
    • Liu, H.1    Ji, M.2    Jiang, H.3    Liu, L.4    Hua, W.5    Chen, K.6    Ji, R.7
  • 34
    • 0035172167 scopus 로고    scopus 로고
    • YUA001, a novel aldose reductase inhibitor isolated from alkalophilic corynebacterium sp. YUA25 II. Chemical modification and biological activity
    • Sun, W. S.; Lee, H. S.; Park, J. M.; Kim, S. H.; Yu, J. H.; Kim, J. H. YUA001, a novel aldose reductase inhibitor isolated from alkalophilic corynebacterium sp. YUA25 II. Chemical modification and biological activity. J. Antibiot. 2001, 54, 827-830.
    • (2001) J. Antibiot. , vol.54 , pp. 827-830
    • Sun, W.S.1    Lee, H.S.2    Park, J.M.3    Kim, S.H.4    Yu, J.H.5    Kim, J.H.6
  • 35
    • 0028869712 scopus 로고
    • Convenient synthesis of tertiary amines by alkylation of secondary amines with alkyl halides in the presence of potassium hydride and triethylamine
    • Mohri, K.; Suzuku, K.; Usui, M.; Isobe, K.; Tsuda, Y. Convenient synthesis of tertiary amines by alkylation of secondary amines with alkyl halides in the presence of potassium hydride and triethylamine. Chem. Pharm. Bull. 1995, 43, 159-161.
    • (1995) Chem. Pharm. Bull. , vol.43 , pp. 159-161
    • Mohri, K.1    Suzuku, K.2    Usui, M.3    Isobe, K.4    Tsuda, Y.5
  • 36
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • Rarey, M.; Kramer, B.; Lengauer, T.; Klebe, G. A fast flexible docking method using an incremental construction algorithm. J. Mol. Biol. 1996, 261, 470-489.
    • (1996) J. Mol. Biol. , vol.261 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 37
    • 0032738842 scopus 로고    scopus 로고
    • Evaluation of the FLEXX incremental construction algorithm for protein-ligand docking
    • Kramer, B.; Rarey, M.; Lengauer, T. Evaluation of the FLEXX incremental construction algorithm for protein-ligand docking. Proteins 1999, 37, 228-241.
    • (1999) Proteins , vol.37 , pp. 228-241
    • Kramer, B.1    Rarey, M.2    Lengauer, T.3
  • 38
    • 0031570301 scopus 로고    scopus 로고
    • A specificity pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil
    • Urzhumtsev, A.; Tete, F. A.; Mitschler, A.; Barbanton, J.; Barth, P.; Urzhumtseva, L.; Biellmann, J. F.; Podjarny, A.; Moras, D. A specificity pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil. Structure 1997, 5, 601-612.
    • (1997) Structure , vol.5 , pp. 601-612
    • Urzhumtsev, A.1    Tete, F.A.2    Mitschler, A.3    Barbanton, J.4    Barth, P.5    Urzhumtseva, L.6    Biellmann, J.F.7    Podjarny, A.8    Moras, D.9
  • 39
    • 84986432941 scopus 로고
    • Automated docking with grid-based energy evaluation
    • Meng, E. C.; Shoichet, B. K.; Kuntz, I. D. Automated docking with grid-based energy evaluation. J. Comput. Chem. 1992, 13, 505-524.
    • (1992) J. Comput. Chem. , vol.13 , pp. 505-524
    • Meng, E.C.1    Shoichet, B.K.2    Kuntz, I.D.3
  • 41
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • Eldridge, M. D.; Murray, C. W.; Auton, T. R.; Paolini, G. V.; Mee, R. P. Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes J. Computer-Aided Mol. Des. 1997, 11, 425-445.
    • (1997) J. Computer-Aided Mol. Des. , vol.11 , pp. 425-445
    • Eldridge, M.D.1    Murray, C.W.2    Auton, T.R.3    Paolini, G.V.4    Mee, R.P.5
  • 43
    • 0023751431 scopus 로고
    • Comparative molecular field analysis (CoMFA). 1. Effect of shape on binding of steroids to carrier proteins
    • Cramer, R. D. III; Patterson, D. E.; Bunce, J. D.; Comparative molecular field analysis (CoMFA). 1. Effect of shape on binding of steroids to carrier proteins. J. Am. Chem. Soc. 1988, 110, 5959-5967.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 5959-5967
    • Cramer III, R.D.1    Patterson, D.E.2    Bunce, J.D.3
  • 44
    • 0027944195 scopus 로고
    • Molecular similarity indices in a comparative analysis (CoMSIA) of drug molecules to correlate and predict their biological activity
    • Klebe, G.; Abraham, U.; Mietzner, T. Molecular similarity indices in a comparative analysis (CoMSIA) of drug molecules to correlate and predict their biological activity. J. Med. Chem. 1994, 37, 4130-4146.
    • (1994) J. Med. Chem. , vol.37 , pp. 4130-4146
    • Klebe, G.1    Abraham, U.2    Mietzner, T.3
  • 45
    • 0033022163 scopus 로고    scopus 로고
    • Comparative molecular similarity index analysis (CoMSIA) to study hydrogen-bonding properties and to score combinatorial libraries
    • Klebe, G.; Abraham, U. Comparative molecular similarity index analysis (CoMSIA) to study hydrogen-bonding properties and to score combinatorial libraries. J. Comput.-Aided Mol. Des. 1999, 13, 1-10.
    • (1999) J. Comput.-Aided Mol. Des. , vol.13 , pp. 1-10
    • Klebe, G.1    Abraham, U.2
  • 46
    • 0342368665 scopus 로고    scopus 로고
    • Structure-based 3D-QSAR-merging the accuracy of structure-based alignment with the computational efficiency of ligand-based methods
    • Sippl, W.; Höltje, H.-D. Structure-based 3D-QSAR-merging the accuracy of structure-based alignment with the computational efficiency of ligand-based methods. Journal of Molecular Structure: Theochem 2000, 503, 31-50.
    • (2000) Journal of Molecular Structure: Theochem. , vol.503 , pp. 31-50
    • Sippl, W.1    Höltje, H.-D.2


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