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Volumn 49, Issue 14, 2006, Pages 4409-4424

Novel selective inhibitors of neutral endopeptidase for the treatment of female sexual arousal disorder. Synthesis and activity of functionalized glutaramides

Author keywords

[No Author keywords available]

Indexed keywords

AMOXICILLIN; BACLOFEN; CADOXATRILAT; CIPROFLOXACIN; DICLOFENAC; ENKEPHALINASE INHIBITOR; FLUINDOSTATIN; FLURBIPROFEN; FUROSEMIDE; GABAPENTIN; GLUTARAMIC ACID DERIVATIVE; IBUPROFEN; KETOPROFEN; SULINDAC; TOLMETIN; UNCLASSIFIED DRUG;

EID: 33745872565     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm060133g     Document Type: Article
Times cited : (32)

References (47)
  • 2
    • 0031834326 scopus 로고    scopus 로고
    • Definition and classification of female sexual disorders
    • Leiblum, S. R. Definition and Classification of Female Sexual Disorders. Int. J. Impotence Res. 1998, 10, S104-S106.
    • (1998) Int. J. Impotence Res. , vol.10
    • Leiblum, S.R.1
  • 3
    • 0018184279 scopus 로고
    • Frequency of sexual dysfunction in 'normal' couples
    • (a) Frank, E.; Anderson, C.; Rubinstein, D. Frequency of Sexual Dysfunction in 'Normal' Couples. N. Eng. J. Med. 1978, 299, 111-115.
    • (1978) N. Eng. J. Med. , vol.299 , pp. 111-115
    • Frank, E.1    Anderson, C.2    Rubinstein, D.3
  • 5
    • 0031805041 scopus 로고    scopus 로고
    • Vasculogenic female sexual dysfunction: Vaginal engorgement and clitoral erectile insufficiency syndromes
    • (a) Goldstein, I.; Berman, J. R. Vasculogenic Female Sexual Dysfunction: Vaginal Engorgement and Clitoral Erectile Insufficiency Syndromes. Int. J. Impotence Res. 1998, 10, S84-S90.
    • (1998) Int. J. Impotence Res. , vol.10
    • Goldstein, I.1    Berman, J.R.2
  • 6
    • 0030903202 scopus 로고    scopus 로고
    • Vasculogenic female sexual dysfunction: The haemodynamic basis for vaginal engorgement and clitoral erectile insufficiency
    • (b) Park, K.; Goldstein, I.; Andry, C.; Siroky, M. B.; Krane, R. J.; Azadzoi, K. M. Vasculogenic Female Sexual Dysfunction: The Haemodynamic Basis for Vaginal Engorgement and Clitoral Erectile Insufficiency. Int. J. Impotence Res. 1997, 9, 27-37.
    • (1997) Int. J. Impotence Res. , vol.9 , pp. 27-37
    • Park, K.1    Goldstein, I.2    Andry, C.3    Siroky, M.B.4    Krane, R.J.5    Azadzoi, K.M.6
  • 7
    • 0020565661 scopus 로고
    • Vasoactive intestinal polypeptide (VIP) increases vaginal blood flow and inhibits uterine smooth muscle activity in women
    • (a) Ottesen, B.; Gertenberg, T.; Ulrichsen, H.; Manthorpe, T. Fahrenkrug, J.; Wagner, G. Vasoactive Intestinal Polypeptide (VIP) Increases Vaginal Blood Flow and Inhibits Uterine Smooth Muscle Activity in Women. Eur. J. Clin. Invest. 1983, 13, 321-324.
    • (1983) Eur. J. Clin. Invest. , vol.13 , pp. 321-324
    • Ottesen, B.1    Gertenberg, T.2    Ulrichsen, H.3    Manthorpe, T.4    Fahrenkrug, J.5    Wagner, G.6
  • 9
    • 0023410171 scopus 로고
    • Vasoactive intestinal polypeptide (VIP) provokes vaginal lubrication in normal women
    • (c) Ottesen, B.; Pedersen, B.; Nielsen, J.; Dalgaard, D.; Wagner, G.; Fahrenkrug, J. Vasoactive Intestinal Polypeptide (VIP) Provokes Vaginal Lubrication in Normal Women. Peptides 1987, 8, 797-800.
    • (1987) Peptides , vol.8 , pp. 797-800
    • Ottesen, B.1    Pedersen, B.2    Nielsen, J.3    Dalgaard, D.4    Wagner, G.5    Fahrenkrug, J.6
  • 11
    • 0006826135 scopus 로고    scopus 로고
    • Design and pharmacology of dual angiotensin-converting enzyme and neutral endopeptidase inhibitors
    • See for example, (a) De Lombaert, S.; Chatelain, R. E.; Fink, C. A.; Trapani, A. J. Design and Pharmacology of Dual Angiotensin-Converting Enzyme and Neutral Endopeptidase Inhibitors. Curr. Pharm. Des. 1996, 2, 443-462.
    • (1996) Curr. Pharm. Des. , vol.2 , pp. 443-462
    • De Lombaert, S.1    Chatelain, R.E.2    Fink, C.A.3    Trapani, A.J.4
  • 13
    • 0032948546 scopus 로고    scopus 로고
    • The endopeptidase inhibitor, candoxatril, and its therapeutic potential in the treatment of chronic cardiac failure in man
    • McDowell, G.; Nicholls, D. P. The Endopeptidase Inhibitor, Candoxatril, and Its Therapeutic Potential in the Treatment of Chronic Cardiac Failure in Man. Expert Opin. Invest. Drug. 1999, 8, 79-84.
    • (1999) Expert Opin. Invest. Drug. , vol.8 , pp. 79-84
    • McDowell, G.1    Nicholls, D.P.2
  • 15
    • 0031022687 scopus 로고    scopus 로고
    • Oral absorption of β-lactams by intestinal peptide transport proteins
    • Dantzig, A. H. Oral Absorption of β-Lactams by Intestinal Peptide Transport Proteins. Adv. Drug Deliver Rev. 1997, 23, 63-76.
    • (1997) Adv. Drug Deliver Rev. , vol.23 , pp. 63-76
    • Dantzig, A.H.1
  • 17
    • 0015973588 scopus 로고
    • Purification and specificity of a neutral endopeptidase from rabbit kidney brush border
    • Kerr, M. A.; Kenny, A. J. Purification and Specificity of a Neutral Endopeptidase from Rabbit Kidney Brush Border. Biochem J. 1974, 137, 477-488.
    • (1974) Biochem J. , vol.137 , pp. 477-488
    • Kerr, M.A.1    Kenny, A.J.2
  • 18
    • 0034681296 scopus 로고    scopus 로고
    • Structure of human neutral endopeptidase (neprilysin) complexed with phosphoramidon
    • Oefner, C.; D'Arcy, A.; Henning, M.; Winkler, F. K.; Dale, G. E. Structure of Human Neutral Endopeptidase (Neprilysin) Complexed with Phosphoramidon. J. Mol. Biol. 2000, 296, 341-349.
    • (2000) J. Mol. Biol. , vol.296 , pp. 341-349
    • Oefner, C.1    D'Arcy, A.2    Henning, M.3    Winkler, F.K.4    Dale, G.E.5
  • 19
    • 0024580983 scopus 로고
    • Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin
    • (a) Roderick, S. L.; Foumie-Zaluski, M. C.; Roques, B. P.; Matthews, B. W. Thiorphan and Retro-Thiorphan Display Equivalent Interactions When Bound to Crystalline Thermolysin. Biochemistry 1989, 28, 1493-1497.
    • (1989) Biochemistry , vol.28 , pp. 1493-1497
    • Roderick, S.L.1    Foumie-Zaluski, M.C.2    Roques, B.P.3    Matthews, B.W.4
  • 20
    • 33845280830 scopus 로고
    • Structural basis of the action of thermolysin and related zinc peptidases
    • (b) Matthews, B. W. Structural Basis of the Action of Thermolysin and Related Zinc Peptidases. Acc. Chem. Res. 1988, 21, 333-340.
    • (1988) Acc. Chem. Res. , vol.21 , pp. 333-340
    • Matthews, B.W.1
  • 21
    • 0032912508 scopus 로고    scopus 로고
    • A three-dimensional construction of the active site (Region 507-749) of human neutral endopeptidase (EC.3.4.24.11)
    • Tiraboschi, G.; Jullian, N.; Thery, V.; Antonezak, S.; Fournie-Zaluski, M. C.; Roque, B. P. A Three-Dimensional Construction of the Active Site (Region 507-749) of Human Neutral Endopeptidase (EC.3.4.24.11). Protein Eng. 1999, 12, 141-149.
    • (1999) Protein Eng. , vol.12 , pp. 141-149
    • Tiraboschi, G.1    Jullian, N.2    Thery, V.3    Antonezak, S.4    Fournie-Zaluski, M.C.5    Roque, B.P.6
  • 22
    • 18744405679 scopus 로고    scopus 로고
    • Second generation inhibitors for the metalloprotease neprilysin based on bicyclic heteroaromatic scaffolds: Synthesis, biological activity and X-ray crystal structure analysis
    • For a recent study of thiorphan bound in a human NEP Construct see Sahli, S.; Frank, B.; Schweizer, W. B.; Diederich, F.; Blum-Kaelin, D.; Aebi, J. D.; Bohm, H-J.; Oefner, C.; Dale, G. E. Second Generation Inhibitors for the Metalloprotease Neprilysin Based on Bicyclic Heteroaromatic Scaffolds: Synthesis, Biological Activity and X-ray Crystal Structure Analysis. Helv. Chim. Acta 2005, 88,731-750.
    • (2005) Helv. Chim. Acta , vol.88 , pp. 731-750
    • Sahli, S.1    Frank, B.2    Schweizer, W.B.3    Diederich, F.4    Blum-Kaelin, D.5    Aebi, J.D.6    Bohm, H.-J.7    Oefner, C.8    Dale, G.E.9
  • 23
    • 0028158656 scopus 로고
    • Inhibition of thermolysin and neutral endopeptidase 24.11 by a novel glutaramide derivative: X-ray structure determination of the thermolysin-inhibitor complex
    • Holland, D. R.; Barclay, P. L.; Danilewicz, J. C.; Matthews, B. W.; James, K. Inhibition of Thermolysin and Neutral Endopeptidase 24.11 by a Novel Glutaramide Derivative: X-ray Structure Determination of the Thermolysin-Inhibitor Complex. Biochemistry 1994, 33, 51-56.
    • (1994) Biochemistry , vol.33 , pp. 51-56
    • Holland, D.R.1    Barclay, P.L.2    Danilewicz, J.C.3    Matthews, B.W.4    James, K.5
  • 24
    • 33745834536 scopus 로고    scopus 로고
    • note
    • Subsequent studies have investigated cocrystal structures of proprietary inhibitors bound in recombinant human NEP.These studies and compound designs derived from them will be disclosed elsewhere.
  • 25
    • 0033548571 scopus 로고    scopus 로고
    • Stereoselective synthesis of a candoxatril intermediate via asymmetric hydrogenation
    • Challenger, S.; Derrick, A.; Mason, C. P.; Silk. T. Stereoselective Synthesis of a Candoxatril Intermediate via Asymmetric Hydrogenation Tetrahedron Lett. 1999, 40, 2187-2190.
    • (1999) Tetrahedron Lett. , vol.40 , pp. 2187-2190
    • Challenger, S.1    Derrick, A.2    Mason, C.P.3    Silk, T.4
  • 27
    • 0000559215 scopus 로고
    • Studies in the enamine field: Reactions of sulfonyl and nitro-enamines with azides
    • Maiorana, S.; Pocar, D.; Dalla Croce, P. Studies in the Enamine Field: Reactions of Sulfonyl and Nitro-Enamines with Azides. Tetrahedron Lett. 1966, 48, 6043-6045.
    • (1966) Tetrahedron Lett. , vol.48 , pp. 6043-6045
    • Maiorana, S.1    Pocar, D.2    Dalla Croce, P.3
  • 29
  • 30
    • 2842556721 scopus 로고
    • Convenient synthesis of 2.7-disubstituted 5H-1,3,4-thiadiazolo[3.2-a]- pyrimidin-5-ones and related compounds
    • (a) Tadakazu, T.; Keiko, T. Convenient Synthesis of 2.7-Disubstituted 5H-1,3,4-Thiadiazolo[3.2-a]-Pyrimidin-5-ones and Related Compounds. Bull. Chem. Soc. Jpn. 1982, 55, 637-638.
    • (1982) Bull. Chem. Soc. Jpn. , vol.55 , pp. 637-638
    • Tadakazu, T.1    Keiko, T.2
  • 31
    • 33745805682 scopus 로고    scopus 로고
    • US Patent 2,422,050, 1947
    • (b) Steahly, G. W. US Patent 2,422,050, 1947.
    • Steahly, G.W.1
  • 32
    • 0002186050 scopus 로고
    • Asymmetric synthesis of cis-2-substituted cyclohexanamines with high optical purity
    • Frahm, A. W.; Knupp, G. Asymmetric Synthesis of cis-2-Substituted Cyclohexanamines with High Optical Purity. Tetrahedron Lett. 1981, 22, 2633-2636.
    • (1981) Tetrahedron Lett. , vol.22 , pp. 2633-2636
    • Frahm, A.W.1    Knupp, G.2
  • 33
    • 0000868673 scopus 로고
    • Synthesis and absolute configuration of 2-substituted cyclohexylamine
    • Knupp, G.; Frahm, A. W. Synthesis and Absolute Configuration of 2-Substituted Cyclohexylamine. Chem. Ber. 1984, 117, 2076-2098.
    • (1984) Chem. Ber. , vol.117 , pp. 2076-2098
    • Knupp, G.1    Frahm, A.W.2
  • 34
    • 0031243451 scopus 로고    scopus 로고
    • Specific fluorogenic substrates for neprilysin (neutral endopeptidase. EC 3.4.24.11) which are highly resistant to serine- and metalloproteases
    • Medeiros, M. A.; Franca, M. S.; Boileau, G.; Juliano, L.; Carvalho, K. M. Specific Fluorogenic Substrates for Neprilysin (Neutral Endopeptidase. EC 3.4.24.11) which are Highly Resistant to Serine- and Metalloproteases. Braz. J. Med. Biol. Res. 1997, 30, 1157-1162.
    • (1997) Braz. J. Med. Biol. Res. , vol.30 , pp. 1157-1162
    • Medeiros, M.A.1    Franca, M.S.2    Boileau, G.3    Juliano, L.4    Carvalho, K.M.5
  • 35
    • 0016231969 scopus 로고
    • A rapid method for the preparation of microvilli from rabbit kidney
    • Booth, A. G.; Kenny, A. J. A Rapid Method for the Preparation of Microvilli from Rabbit Kidney. Biochem. J. 1974, 142, 575-581.
    • (1974) Biochem. J. , vol.142 , pp. 575-581
    • Booth, A.G.1    Kenny, A.J.2
  • 36
    • 33745829933 scopus 로고    scopus 로고
    • note
    • (a) All LogD values were measured at pH 7.4.
  • 37
    • 0025358815 scopus 로고
    • An improved method for the determination of distribution coefficients
    • (b) Stopher, D.; McClean, S. An Improved Method for the Determination of Distribution Coefficients. J. Pharm. Pharmacol. 1990, 42, 144.
    • (1990) J. Pharm. Pharmacol. , vol.42 , pp. 144
    • Stopher, D.1    McClean, S.2
  • 38
    • 0026733297 scopus 로고
    • Sex difference in the excretion of zenarestat in mice, rats, dogs and humans
    • (a) Tanaka, Y.; Fujiwara, T.; Esumi, Y. Sex Difference in the Excretion of Zenarestat in Mice, Rats, Dogs and Humans. Xenobiotica 1992, 22, 941-947.
    • (1992) Xenobiotica , vol.22 , pp. 941-947
    • Tanaka, Y.1    Fujiwara, T.2    Esumi, Y.3
  • 39
    • 0028937548 scopus 로고
    • Sex-dependent and independent renal excretion of nilvadipine metabolites in rat: Evidence for a sex-dependent active secretion in kidney
    • (b) Terashita, S.; Sawamoto, T.; Deguchi, T.; Tokuma, Y.; Hata, T. Sex-Dependent and Independent Renal Excretion of Nilvadipine Metabolites in Rat: Evidence for a Sex-Dependent Active Secretion in Kidney. Xenobiotica 1995, 25, 37-47.
    • (1995) Xenobiotica , vol.25 , pp. 37-47
    • Terashita, S.1    Sawamoto, T.2    Deguchi, T.3    Tokuma, Y.4    Hata, T.5
  • 40
    • 0034778701 scopus 로고    scopus 로고
    • Sex-related differences in the renal disposition of the acidic metabolite of clentiazem in rats
    • (c) Hanada, K.; Fujisawa, R.; Kataoka, R.; Nakamura, S.; Ogata, H. Sex-Related Differences in the Renal Disposition of the Acidic Metabolite of Clentiazem in Rats. Xenobiotica 2001, 31, 725-731.
    • (2001) Xenobiotica , vol.31 , pp. 725-731
    • Hanada, K.1    Fujisawa, R.2    Kataoka, R.3    Nakamura, S.4    Ogata, H.5
  • 42
    • 0036081327 scopus 로고    scopus 로고
    • Gender difference in the Oatp1-mediated tubular reabsorption of estradiol l7β-D-glucuronide in rats
    • (b) Gotoh, Y.; Kato, Y.; Stieger, B.; Meier, P. J.; Sugiyama, Y. Gender Difference in the Oatp1-Mediated Tubular Reabsorption of Estradiol l7β-D-Glucuronide in Rats. Am. J. Physiol. 2002, 282, E1245-E1254.
    • (2002) Am. J. Physiol. , vol.282
    • Gotoh, Y.1    Kato, Y.2    Stieger, B.3    Meier, P.J.4    Sugiyama, Y.5
  • 43
    • 0031948975 scopus 로고    scopus 로고
    • Sex-dependent metabolism of xenobiotics
    • Mugford, C. A.; Kedderis, G. L. Sex-Dependent Metabolism of Xenobiotics. Drug Metab. Rev. 1998, 30, 441-498.
    • (1998) Drug Metab. Rev. , vol.30 , pp. 441-498
    • Mugford, C.A.1    Kedderis, G.L.2
  • 44
    • 0034933916 scopus 로고    scopus 로고
    • Gender-based differences in pharmacokinetics in laboratory animal models
    • Czerniak, R. Gender-Based Differences in Pharmacokinetics in Laboratory Animal Models. Int. J. Toxicol. 2001, 20, 161-163.
    • (2001) Int. J. Toxicol. , vol.20 , pp. 161-163
    • Czerniak, R.1
  • 45
    • 18544392358 scopus 로고    scopus 로고
    • A review of the physiology and pharmacology of peripheral female genital arousal in the animal model
    • (a) Munarriz, R.; Kim, S. W.; Kim, N. N.; Abdulmaged, T.; Goldstein, I. A Review of the Physiology and Pharmacology of Peripheral Female Genital Arousal in the Animal Model. 2003, J. Urol. 170, S40-S45.
    • (2003) J. Urol. , vol.170
    • Munarriz, R.1    Kim, S.W.2    Kim, N.N.3    Abdulmaged, T.4    Goldstein, I.5
  • 46
    • 33745847955 scopus 로고    scopus 로고
    • Eur. Pat. Appl. EP 1097719, 2001
    • (b) Maw, G. N.; Wayman, C. P. Eur. Pat. Appl. EP 1097719, 2001.
    • Maw, G.N.1    Wayman, C.P.2


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