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Volumn 53, Issue 15, 2010, Pages 5620-5628

Discovery of 6-(Aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2- α]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

6 (AMINOMETHYL) 5 (2,4 DICHLOROPHENYL) 7 METHYLIMIDAZO[1,2 A]PYRIMIDINE 2 CARBOXAMIDE DERIVATIVE; 6 (AMINOMETHYL) 5 (2,4 DICHLOROPHENYL) N (1 ETHYL 1H PYRAZOL 5 YL) 7 METHYLIMIDAZO[1,2 A]PYRIMIDINE 2 CARBOXAMIDE; [6 (AMINOMETHYL) 5 (2,4 DICHLOROPHENYL) 7 METHYLIMIDAZO[1,2 A]PYRIMIDIN 2 YL](MORPHOLINO)METHANONE; DIPEPTIDYL PEPTIDASE IV INHIBITOR; IMIDAZOLE DERIVATIVE; POTASSIUM CHANNEL HERG; SODIUM CHANNEL; UNCLASSIFIED DRUG;

EID: 77955387970     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm100634a     Document Type: Article
Times cited : (44)

References (43)
  • 1
    • 68149161100 scopus 로고    scopus 로고
    • Mining incretin hormone pathways for novel therapies
    • Wideman, R. D.; Kieffer, T. J. Mining incretin hormone pathways for novel therapies Trends Endocrinol. Metab. 2009, 20, 280-286
    • (2009) Trends Endocrinol. Metab. , vol.20 , pp. 280-286
    • Wideman, R.D.1    Kieffer, T.J.2
  • 2
    • 33644676141 scopus 로고    scopus 로고
    • Incretin mimetics and dipeptidyl peptidase-IV inhibitors: Potential new therapies for type 2 diabetes mellitus
    • Triplitt, C.; Wright, A.; Chiquette, E. Incretin mimetics and dipeptidyl peptidase-IV inhibitors: potential new therapies for type 2 diabetes mellitus Pharmacotherapy 2006, 26, 360-374
    • (2006) Pharmacotherapy , vol.26 , pp. 360-374
    • Triplitt, C.1    Wright, A.2    Chiquette, E.3
  • 3
    • 28644443140 scopus 로고    scopus 로고
    • Glucagon-like peptide-1-based therapies for the treatment of type 2 diabetes mellitus
    • DOI 10.2165/00024677-200504060-00005
    • Gallwitz, B. Glucagon-like peptide-1-based therapies for the treatment of type 2 diabetes mellitus Treat. Endocrinol. 2005, 4, 361-370 (Pubitemid 41751172)
    • (2005) Treatments in Endocrinology , vol.4 , Issue.6 , pp. 361-370
    • Gallwitz, B.1
  • 4
    • 0009307846 scopus 로고
    • Glucagon-like peptide-1 (GLP-1) a newly discovered GI hormone
    • Holst, J. J. Glucagon-like peptide-1 (GLP-1) a newly discovered GI hormone Gastroenterology 1994, 107, 1048-1055
    • (1994) Gastroenterology , vol.107 , pp. 1048-1055
    • Holst, J.J.1
  • 5
    • 0031936954 scopus 로고    scopus 로고
    • Glucagon-like peptides
    • Drucker, D. J. Glucagon-like peptides Diabetes 1998, 47, 159-169
    • (1998) Diabetes , vol.47 , pp. 159-169
    • Drucker, D.J.1
  • 6
    • 1842855423 scopus 로고    scopus 로고
    • Incretins, insulin secretion and type 2 diabetes mellitus
    • Vilsboll, T.; Holst, J. J. Incretins, insulin secretion and type 2 diabetes mellitus Diabetologia 2004, 47, 357-366
    • (2004) Diabetologia , vol.47 , pp. 357-366
    • Vilsboll, T.1    Holst, J.J.2
  • 7
    • 0028224617 scopus 로고
    • The insulinotropic actions of glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (7-37) in normal and diabetic subjects
    • Elahi, D.; McAloon-Dyke, M.; Fukagawa, N. K.; Meneilly, G. S.; Sclater, A. L.; Minaker, K. L.; Habener, J. F.; Andersen, D. K. The insulinotropic actions of glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (7-37) in normal and diabetic subjects Regul. Pept. 1994, 51, 63-75
    • (1994) Regul. Pept. , vol.51 , pp. 63-75
    • Elahi, D.1    Mcaloon-Dyke, M.2    Fukagawa, N.K.3    Meneilly, G.S.4    Sclater, A.L.5    Minaker, K.L.6    Habener, J.F.7    Andersen, D.K.8
  • 8
    • 0027419106 scopus 로고
    • Additive insulinotropic effects of exogenous synthetic human gastric inhibitory polypeptide and glucagon-like peptide-1-(7-36) amide infused at near-physiological insulinotropic hormone and glucose concentrations
    • Nauck, M. A.; Bartels, E.; Oerskov, C.; Ebert, R.; Creutzfeldt, W. Additive insulinotropic effects of exogenous synthetic human gastric inhibitory polypeptide and glucagon-like peptide-1-(7-36) amide infused at near-physiological insulinotropic hormone and glucose concentrations J. Clin. Endocrinol. Metab. 1993, 76, 912-917
    • (1993) J. Clin. Endocrinol. Metab. , vol.76 , pp. 912-917
    • Nauck, M.A.1    Bartels, E.2    Oerskov, C.3    Ebert, R.4    Creutzfeldt, W.5
  • 11
    • 0036869408 scopus 로고    scopus 로고
    • Therapy of type 2 diabetes mellitus based on the actions of glucagon-like peptide-1
    • Holst, J. J. Therapy of type 2 diabetes mellitus based on the actions of glucagon-like peptide-1 Diabetes Metab. Res. Rev. 2002, 18, 430-441
    • (2002) Diabetes Metab. Res. Rev. , vol.18 , pp. 430-441
    • Holst, J.J.1
  • 12
    • 0033303516 scopus 로고    scopus 로고
    • Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine
    • Hansen, L.; Deacon, C. F.; Orskov, C.; Holst, J. J. Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine Endocrinology 1999, 140, 5356-5363
    • (1999) Endocrinology , vol.140 , pp. 5356-5363
    • Hansen, L.1    Deacon, C.F.2    Orskov, C.3    Holst, J.J.4
  • 13
    • 0034811909 scopus 로고    scopus 로고
    • Improved glucose tolerance via enhanced glucose-dependent insulin secretion in dipeptidyl peptidase IV-deficient Fischer rats
    • Nagakura, T.; Yasuda, N.; Yamazaki, K.; Ikuta, H.; Yoshikawa, S.; Asano, O.; Tanaka, I. Improved glucose tolerance via enhanced glucose-dependent insulin secretion in dipeptidyl peptidase IV-deficient Fischer rats Biochem. Biophys. Res. Commun. 2001, 284, 501-506
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 501-506
    • Nagakura, T.1    Yasuda, N.2    Yamazaki, K.3    Ikuta, H.4    Yoshikawa, S.5    Asano, O.6    Tanaka, I.7
  • 15
    • 0033852128 scopus 로고    scopus 로고
    • Molecular characterization of dipeptidyl peptidase activity in serum. Soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides
    • Durinx, C.; Lambeir, A.; Bosmans, E.; Falmagne, J.; Berghmans, R.; Haemers, A.; Scharpe, S.; De Meester, I. Molecular characterization of dipeptidyl peptidase activity in serum. Soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides Eur. J. Biochem. 2000, 267, 5608-5613
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5608-5613
    • Durinx, C.1    Lambeir, A.2    Bosmans, E.3    Falmagne, J.4    Berghmans, R.5    Haemers, A.6    Scharpe, S.7    De Meester, I.8
  • 16
    • 0031657655 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV from human serum: Purification, characterization, and N-terminal amino acid sequence
    • Iwaki-Egawa, S.; Watanabe, Y.; Kikuya, Y.; Fujimoto, Y. Dipeptidyl peptidase IV from human serum: purification, characterization, and N-terminal amino acid sequence J. Biochem. 1998, 124, 428-433
    • (1998) J. Biochem. , vol.124 , pp. 428-433
    • Iwaki-Egawa, S.1    Watanabe, Y.2    Kikuya, Y.3    Fujimoto, Y.4
  • 17
    • 0037777695 scopus 로고    scopus 로고
    • 1-[[(3-Hydroxy-1-adamantyl)amino]acetyl]-2-cyano-(S)-pyrrolidine: A potent, selective, and orally bioavailable dipeptidyl peptidase IV inhibitor with antihyperglycemic properties
    • Villhauer, E. B.; Brinkman, J. A.; Naderi, G. B.; Burkey, B. F.; Dunning, B. E.; Prasad, K.; Mangold, B. L.; Russell, M. E.; Hughes, T. E. 1-[[(3-Hydroxy-1-adamantyl)amino]acetyl]-2-cyano-(S)-pyrrolidine: A potent, selective, and orally bioavailable dipeptidyl peptidase IV inhibitor with antihyperglycemic properties J. Med. Chem. 2003, 46, 2774-2789
    • (2003) J. Med. Chem. , vol.46 , pp. 2774-2789
    • Villhauer, E.B.1    Brinkman, J.A.2    Naderi, G.B.3    Burkey, B.F.4    Dunning, B.E.5    Prasad, K.6    Mangold, B.L.7    Russell, M.E.8    Hughes, T.E.9
  • 21
    • 61349143225 scopus 로고    scopus 로고
    • Medicinal chemistry approaches to the inhibition of dipeptidyl peptidase-4 for the treatment of type 2 diabetes
    • For other small molecular DPP4 inhibitors, see;, and references cited therein.
    • For other small molecular DPP4 inhibitors, see Havale, S. H.; Pal, M. Medicinal chemistry approaches to the inhibition of dipeptidyl peptidase-4 for the treatment of type 2 diabetes Bioorg. Med. Chem. 2009, 17, 1783-1802 and references cited therein.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 1783-1802
    • Havale, S.H.1    Pal, M.2
  • 22
    • 77955367308 scopus 로고    scopus 로고
    • Synthesis and SAR of azolopyrimidines as potent and selective dipeptidyl peptidase-4 (DPP4) inhibitors for type 2 diabetes
    • 4398.
    • Brigance, R. P.; Meng, W.; Fura, A.; Harrity, T.; Wang, A.; Zahler, R.; Kirby, M. S.; Hamman, L. G. Synthesis and SAR of azolopyrimidines as potent and selective dipeptidyl peptidase-4 (DPP4) inhibitors for type 2 diabetes. Bioorg. Med. Chem. Lett. 2010, 20, 4395 - 4398.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 4395
    • Brigance, R.P.1    Meng, W.2    Fura, A.3    Harrity, T.4    Wang, A.5    Zahler, R.6    Kirby, M.S.7    Hamman, L.G.8
  • 23
    • 0028220833 scopus 로고
    • Research on heterocyclic compounds. XXXII. Synthesis and cyclooxygenase-independent antiinflammatory and analgesic activity of imidazo[1,2- a ]pyrimidine derivatives
    • Abignente, E.; Sacchi, A.; Laneri, S.; Rossi, F.; D'Amico, M.; Berrino, L.; Calderaro, V.; Parrillo, C. Research on heterocyclic compounds. XXXII. Synthesis and cyclooxygenase-independent antiinflammatory and analgesic activity of imidazo[1,2- a ]pyrimidine derivatives Eur. J. Med. Chem. 1994, 29, 279-286
    • (1994) Eur. J. Med. Chem. , vol.29 , pp. 279-286
    • Abignente, E.1    Sacchi, A.2    Laneri, S.3    Rossi, F.4    D'amico, M.5    Berrino, L.6    Calderaro, V.7    Parrillo, C.8
  • 24
    • 77955351459 scopus 로고
    • Preparation of bis(N -protected)-2-aminoimidazole-4-carboxaldehyde
    • pp. FR 2681323.
    • Commercon, A. Preparation of bis(N -protected)-2-aminoimidazole-4- carboxaldehyde. Fr. Demande 1993, 12 pp. FR 2681323.
    • (1993) Fr. Demande , pp. 12
    • Commercon, A.1
  • 26
    • 0033780088 scopus 로고    scopus 로고
    • Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8
    • Abbott, C. A.; Yu, D. M. T.; Woollatt, E.; Sutherland, G. R.; McCaughan, G. W.; Gorrell, M. D. Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8 Eur. J. Biochem. 2000, 267, 6140-6150
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6140-6150
    • Abbott, C.A.1    Yu, D.M.T.2    Woollatt, E.3    Sutherland, G.R.4    Mccaughan, G.W.5    Gorrell, M.D.6
  • 28
    • 0037121086 scopus 로고    scopus 로고
    • Identification and characterization of human DPP9, a novel homologue of dipeptidyl peptidase IV
    • Olsen, C.; Wagtmann, N. Identification and characterization of human DPP9, a novel homologue of dipeptidyl peptidase IV Gene 2002, 299, 185-193
    • (2002) Gene , vol.299 , pp. 185-193
    • Olsen, C.1    Wagtmann, N.2
  • 29
    • 3042734543 scopus 로고    scopus 로고
    • Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity
    • Ajami, K.; Abbott, C., A.; McCaughan, G., W.; Gorrell, M., D. Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity Biochim. Biophys. Acta 2004, 1679, 18-28
    • (2004) Biochim. Biophys. Acta , vol.1679 , pp. 18-28
    • Ajami, K.1    Abbott, C..A.2    Mccaughan, G..W.3    Gorrell, M..D.4
  • 30
    • 14844329054 scopus 로고    scopus 로고
    • Kinetic investigation of human dipeptidyl peptidase II (DPPII)-mediated hydrolysis of dipeptide derivatives and its identification as quiescent cell proline dipeptidase (QPP)/dipeptidyl peptidase 7 (DPP7)
    • Maes, M. B.; Lambeir, A. M.; Gilany, K.; Senten, K.; Van der veken, P.; Leiting, B.; Augustyns, K.; Scharpe, S.; De Meester, I. Kinetic investigation of human dipeptidyl peptidase II (DPPII)-mediated hydrolysis of dipeptide derivatives and its identification as quiescent cell proline dipeptidase (QPP)/dipeptidyl peptidase 7 (DPP7) Biochem. J. 2005, 386, 315-324
    • (2005) Biochem. J. , vol.386 , pp. 315-324
    • Maes, M.B.1    Lambeir, A.M.2    Gilany, K.3    Senten, K.4    Van Der Veken, P.5    Leiting, B.6    Augustyns, K.7    Scharpe, S.8    De Meester, I.9
  • 31
    • 0035110501 scopus 로고    scopus 로고
    • Purification, molecular cloning, and immunohistochemical localization of dipeptidyl peptidase II from the rat kidney and its identity with quiescent cell proline dipeptidase
    • Araki, H.; Li, Y. H.; Yamamoto, Y.; Haneda, M.; Nishi, K.; Kikkawa, R.; Ohkubo, I. Purification, molecular cloning, and immunohistochemical localization of dipeptidyl peptidase II from the rat kidney and its identity with quiescent cell proline dipeptidase J. Biochem. 2001, 129, 279-288
    • (2001) J. Biochem. , vol.129 , pp. 279-288
    • Araki, H.1    Li, Y.H.2    Yamamoto, Y.3    Haneda, M.4    Nishi, K.5    Kikkawa, R.6    Ohkubo, I.7
  • 32
    • 70549090998 scopus 로고    scopus 로고
    • Diverse functions in a conserved structure: The dipeptidyl peptidase IV gene family
    • In;, Ed.; Nova Science Publishers, Inc.: Hauppauge, NY,; pp - 78.
    • Gorrell, M. D.; Yu, D. M. T. Diverse functions in a conserved structure: the dipeptidyl peptidase IV gene family. In Trends in Protein Research; Robinson, J. W., Ed.; Nova Science Publishers, Inc.: Hauppauge, NY, 2005; pp 1 - 78.
    • (2005) Trends in Protein Research , pp. 1
    • Gorrell, M.D.1    Yu, D.M.T.2    Robinson, J.W.3
  • 36
    • 13844254976 scopus 로고    scopus 로고
    • Predictive in silico modeling for hERG channel blockers
    • Aronov, A. M. Predictive in silico modeling for hERG channel blockers Drug Discovery Today 2005, 10, 149-155
    • (2005) Drug Discovery Today , vol.10 , pp. 149-155
    • Aronov, A.M.1
  • 37
    • 33244474244 scopus 로고    scopus 로고
    • Development and evaluation of an in silico model for hERG binding
    • Song, M.; Clark, M. Development and evaluation of an in silico model for hERG binding J. Chem. Inf. Model 2006, 46, 392-400
    • (2006) J. Chem. Inf. Model , vol.46 , pp. 392-400
    • Song, M.1    Clark, M.2
  • 38
    • 27744443484 scopus 로고    scopus 로고
    • Human ether-a-go-go related gene (HERG): A chemist's perspective
    • Vaz, R. J.; Li, Y.; Rampe, D. Human ether-a-go-go related gene (HERG): A chemist's perspective Prog. Med. Chem. 2005, 43, 1-18
    • (2005) Prog. Med. Chem. , vol.43 , pp. 1-18
    • Vaz, R.J.1    Li, Y.2    Rampe, D.3
  • 39
    • 77955348356 scopus 로고    scopus 로고
    • The X-ray crystal structure coordinates of 24c (BMS-762382) in DPP4 are deposited in the Protein Data Bank (PDB code 3NOX).
    • The X-ray crystal structure coordinates of 24c (BMS-762382) in DPP4 are deposited in the Protein Data Bank (PDB code 3NOX).
  • 41
    • 0042131827 scopus 로고    scopus 로고
    • Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV
    • Thoma, R.; Loffler, B.; Stihle, M.; Huber, W.; Ruf, A.; Hennig, M. Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV Structure 2003, 11, 947-959
    • (2003) Structure , vol.11 , pp. 947-959
    • Thoma, R.1    Loffler, B.2    Stihle, M.3    Huber, W.4    Ruf, A.5    Hennig, M.6
  • 43
    • 70549096922 scopus 로고    scopus 로고
    • Inhibitor selectivity in the clinical application of dipeptidyl peptidase-4 inhibition
    • Kirby, M.; Yu, D. M. T.; O'Connor, S. P.; Gorrell, M. D. Inhibitor selectivity in the clinical application of dipeptidyl peptidase-4 inhibition Clin. Sci. 2010, 118, 31-41
    • (2010) Clin. Sci. , vol.118 , pp. 31-41
    • Kirby, M.1    Yu, D.M.T.2    O'connor, S.P.3    Gorrell, M.D.4


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