Novel N-substituted-2-cyanopyrrolidines as potent inhibitors of dipeptidyl peptidase IV in the treatment of non-insulin-dependent diabetes mellitus

Bibliography

• HEINS J, WELKER P, SCHONLEIN C et al.: Mechanism of proline-specific proteinases: (I) substrate specificity of dipeptidyl peptidase IV from pig kidney and proline-specific endopeptidase from Flavobacterium meningosepticum. Biochim. Biophys. Acta (1988) 954 (2):161–169.
   PubMedGoogle Scholar
• HEGEN M, NIEDOBITEK G, KLEIN C, STEIN H, FLEISCHER B: The T cell triggering molecule Tp103 is associated with dipeptidyl aminopeptidase IV Activity. J. Immunol. (1990) 144(8):2908–2914.
   PubMedGoogle Scholar
• MENTLEIN R, GALLWITZ B, SCHMIDT WE: Dipeptidyl-peptidase W hydrolyses gastric inhibitory polypep-tide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum. Eur. J. Biochem. (1993) 214 (3):829–835.
   PubMedGoogle Scholar
• DE MEESTER I, KOROM S, VAN DAMME J, SCHARPE S: CD26, let it cut or cut it down. Immunol. Today (1999) 20 (8):367–375.
   PubMedGoogle Scholar
• SCHON E, BORN I, DEMUTH HU et al: Dipeptidyl peptidase Win the immune system. effects of specific enzyme inhibitors on activity of dipeptidyl peptidase IV and proliferation of human lymphocytes. Biol. Chem. Hoppe Seyler (1991) 372(5):305–311.
   Google Scholar
• MORIMOTO C SCHLOSSMAN SF: The structure and function of CD26 in the T-cell immune response. Immunol. Rev. (1998) 161:55–70.
   PubMedGoogle Scholar
• WESLEY UV, ALBINO AP, TIWARI S, HOUGHTON AN: A role for dipeptidyl peptidase W in suppressing the malignant phenotype of melanocytic cells. J Exp. Med. (1999) 190(3):311–322.
   PubMedGoogle Scholar
• FLENTKE GR, MUNOZ E, HUBER BT, PLAUT AG, KETTNERCA, BACHOVCHIN WW: Inhibition of dipeptidyl aminopeptidase W (DP-IV) by Xaa-boropro dipep tides and use of these inhibitors to examine the role of DP-Win T-cell function. Proc. Natl. Acad. ScL USA (1991) 88 (4):1556–1559.
   PubMed Web of Science ®Google Scholar
• FLEISCHER B: CD26: a surface protease involved in T-cell activation. Immunol Today (1994) 15 (4) :180–184.
   PubMedGoogle Scholar
• KUBOTA T, FLENTKE GR, BACHOVCHIN WW, STOLLAR BD: Involvement of dipeptidyl peptidase W in an in vivo immune response. Clin. Exp. Immunol. (1992) 89(2):192–197.
   PubMedGoogle Scholar
• HOLST JJ: Glucagon-like peptide 1 (GLP-1): an intestinal hormone, signalling nutritional abundance, with an unusual therapeutic potential. Trends Endocrinol. Metab. (1999) i0(6):229–235.
   Google Scholar
• ZHANG BB, MOLLER DE: New approaches in the treatment of Type 2 Diabetes. Curr. Opin. Chem. Biol. (2000) 4(4):461–467.
   PubMed Web of Science ®Google Scholar
• BAILEY CJ: Potential new treatments for Type 2 diabetes. Trends Pharmacol. ScL (2000) 21(7):259–265.
   PubMedGoogle Scholar
• KNUDSEN LB, PRIDAL L: Glucagon-like pep tide-1 -(9-36) amide is a major metabolite of glucagon-like peptide-147-36) amide after in vivo administration to dogs and it acts as an antagonist on the pancreatic receptor. Eur.J. Pharmacol (1996) 318(2-3):429–435.
   PubMed Web of Science ®Google Scholar
• DEACON CF, JOHNSEN AH, HOLST JJ: Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo. J. Clin. Endocrinol. Metab. (1995) 80 (3):952–957.
   PubMed Web of Science ®Google Scholar
• DEACON CF, NAUCK MA, TOFT-NIELSEN M, PRIDAL L,WILLMS B, HOLST JJ: Both subcutaneously and intrave-nously administered glucagon-like peptide I are rapidly degraded from the NI-12-terminus in Type II diabetic patients and in healthy subjects. Diabetes (1995) 44(9):1126–1131.
   PubMed Web of Science ®Google Scholar
• MARGUET D, BAGGIO L, KOBAYASHI T et al.: Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26. Proc. Natl. Acad. ScL USA (2000) 97 (12):6874–6879.
   PubMed Web of Science ®Google Scholar
• HOLST JJ, DEACON CF: Inhibition of the activity of dipeptidyl-peptidase W as a treatment for Type 2 diabetes. Diabetes (1998) 47(10:1663–1670.
   PubMed Web of Science ®Google Scholar
• DEACON CF, HUGHES TE, HOLST JJ: Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig. Diabetes (1998) 47(5):764–769.
   PubMed Web of Science ®Google Scholar
• ELLIOTT R, MORGAN L, TREDGER J, DEACON S, WRIGHT J, MARKS V: Glucagon-like peptide-1 (7–36)amide and glucose-dependent insulinotropic polypeptide secretion in response to nutrient ingestion in man: acute post-Prandial and 24-h secretion patterns. J Endocrinol. (1993) i38(1):159–166.
   Google Scholar
• ORSKOV C, WETTERGREN A, HOLST JJ: Secretion of the incretin hormones glucagon-like peptide-1 and gastric inhibitory polypeptide correlates with insulin secretion in normal man throughout the day. Scand. Gastroenterol (1996) 31 (7):665–670.
   PubMed Web of Science ®Google Scholar
• COUTTS SJ, KELLY TA, SNOW RJ et al.: Structure-activity relationships of boronic acid inhibitors of dipeptidyl peptidase IV. 1. variation of the P2 position of xaa-boropro dipeptides. J. Med. Chem. (1996) 39(10)2087–2094.
   Google Scholar
• KELLY TA, ADAMS J, BACHOVCHIN WW et al.: Inimun o-sup presiv e boronic acid dipeptides: correlation between conformation and activity. J. Am. Chem. Soc. (1993) 115:12637–12638.
   Google Scholar
• SNOW RJ, BACHOVCHIN WW, BARTON RW et al.: Studies on proline boronic acid dipeptide inhibitors of dipeptidyl peptidase IV: identification of a cyclic species containing a B-Nbond. J. Am. Chem. Soc. (1994) 116:10860–10869.
   Google Scholar
• SUDMEIER JL, GUNTHER UL, GUTHEIL WG et al: Solution structures of active and inactive forms of the Dp IV (Cd26) inhibitor Pro-boropro determined by NMR spectroscopy. Biochemistry (1994) 33 (41) :12427–12438.
   PubMedGoogle Scholar
• BODUSZEK B, OLEKSYSZYN J, KAM CM, SELZLER J, SMITH RE, POWERS JC: Dipeptide phosphonates as inhibitors of dipeptidyl peptidase IV. J. Med. Chem. (1994) 37 (23):3969–3976.
   PubMedGoogle Scholar
• HAEMERS A, DE RANTER A, BELYAEV A et al: A newsynthetic method for proline diphenylphosphonates. Tetrahedron Lett. (1995) 36 (21):3755–3758.
   Google Scholar
• LAMBEIR AM, BORLOO M, DE MEESTER I et al.:Dipeptide-derived diphenyl phosphonate esters: mechanism-based inhibitors of dipeptidyl peptidase IV. Biochim. Biophys. Acta (1996) i290(1):76–82.
   Google Scholar
• DEMUTH HU, BAUMGRASS R, SCHAPER C, FISCHER G, BARTH A: Dipeptidylpeptidase W-inactivation with N-peptidy1-0-aroyl hydroxylamines. J. Enzyme Inhib. (1988) 2 (2) :129–142.
   PubMedGoogle Scholar
• AUGUSTYNS KJL, LAMBEIR AM, BORLOO M et al.: Pyrrolidides: synthesis and structure-activity relation-ship as inhibitors of dipeptidyl peptidase IV. Eur. Med. Chem. (1997) 32(4):301–309.
   Google Scholar
• ASHWORTH DM, ATRASH B, BAKER GR et al.: 2-Cyanopyrrolidides as potent, stable inhibitors of dipeptidyl peptidase W. Bioorg. Med. Chem. Lett. (1996) 6 (10):1163–1166.
   Google Scholar
• LI J, WILK E, WILK S: Aminoacylpyrrolidine-2-nitriles: potent and stable inhibitors of dipeptidyl-peptidase IV (Cd 26). Arch. Biochem. Biophys. (1995) 323 (1):148–154.
   PubMedGoogle Scholar
• HUGHES TE, MONE MD, RUSSELL ME, WELDON SC, VILLHAUER EB: NVP-DPP728 (1 -[[[2 -[(5 -cy an o pyridin - 2 -yl)amin o]ethyliamin o]acety1]-2-cyan o -(5)-pyrrolidine), a slow-binding inhibitor of dipeptidyl peptidase IV. Biochemistry (1999) 38 (36):11597–11603.
   PubMedGoogle Scholar
• REISHER SR, HUGHES TE, ORDOVAS JM, SCHAEFER EJ, FEINSTEIN SI: Increased expression of apolipoprotein genes accompanies differentiation in the intestinal cell line Caco-2. Proc. Natl. Acad. ScL USA (1993) 90 (12):5757–5761.
   PubMedGoogle Scholar
• DAVIES WL, GRUNERT RR, HAFF RF et al.: Antiviral activity of 1 -adamantanamine (amantadine). Science (1964) 144:862–863.
   PubMed Web of Science ®Google Scholar
• KOLOCOURIS A, TATARIDIS D, FYTAS G et al.: Synthesis of 2-(2-adamantyl)piperidines and structure anti-influenza virus a activity relationship study using a combination of NMR spectroscopy and molecular modeling. Bioorg. Med. Chem. Lett. (1999) 9(24)3465–3470.
   Google Scholar
• PEROLA E, CELLAI L, BRUFANI M: Synthesis and activity studies of N-[-N'-(adamant-lt-Y1)aminoalkyl]-2-(4t-dimethylaminophenypacetamides: in the search of selective inhibitors for the different molecular forms of acetylcholinesterase. Bioorg. Med. Chem. Lett. (1998) 8(6)575–580.
   Google Scholar
• SUPURAN CT, MINCIONE F, SCOZZAFAVA A, BRIGANTI F, MINCIONE G, ILIES MA: Carbonic anhydrase inhibitors - Part 52. Metal complexes of heterocyclic sulfona-mides: a new class of strong topical intraocular pressure-lowering agents in rabbits. Eur. J. Med. Chem. (1998) 33(4):247–254.
   Google Scholar