Target-mediated metabolism and target-mediated drug disposition of the DPPIV inhibitor AMG 222

References

• Ahrén B. (2008). Emerging dipeptidyl peptidase-4 inhibitors for the treatment of diabetes. Expert Opin Emerg Drugs 13:593–607.
   PubMed Web of Science ®Google Scholar
• Augustyns K, Van der Veken P, Senten K, Haemers A. (2005). The therapeutic potential of inhibitors of dipeptidyl peptidase IV (DPP IV) and related proline-specific dipeptidyl aminopeptidases. Curr Med Chem 12:971–998.
   PubMed Web of Science ®Google Scholar
• Beconi MG, Reed JR, Teffera Y, Xia YQ, Kochansky CJ, Liu DQ, Xu S, Elmore CS, Ciccotto S, Hora DF, Stearns RA, Vincent SH. (2007). Disposition of the dipeptidyl peptidase 4 inhibitor sitagliptin in rats and dogs. Drug Metab Dispos 35:525–532.
   PubMed Web of Science ®Google Scholar
• Bohannon N. (2009). Overview of the gliptin class (dipeptidyl peptidase-4 inhibitors) in clinical practice. Postgrad Med 121:40–45.
   PubMed Web of Science ®Google Scholar
• Brandt I, Joossens J, Chen X, Maes MB, Scharpé S, De Meester I, Lambeir AM. (2005). Inhibition of dipeptidyl-peptidase IV catalyzed peptide truncation by Vildagliptin ((2S)-{[(3-hydroxyadamantan-1-yl)amino]acetyl}-pyrrolidine-2-carbonitrile). Biochem Pharmacol 70:134–143.
   PubMed Web of Science ®Google Scholar
• Davis JA, Singh S, Sethi S, Roy S, Mittra S, Rayasam G, Bansal V, Sattigeri J, Ray A. (2010). Nature of action of Sitagliptin, the dipeptidyl peptidase-IV inhibitor in diabetic animals. Indian J Pharmacol 42:229–233.
   PubMedGoogle Scholar
• Feng J, Zhang Z, Wallace MB, Stafford JA, Kaldor SW, Kassel DB, Navre M, Shi L, Skene RJ, Asakawa T, Takeuchi K, Xu R, Webb DR, Gwaltney SL 2nd. (2007). Discovery of alogliptin: A potent, selective, bioavailable, and efficacious inhibitor of dipeptidyl peptidase IV. J Med Chem 50:2297–2300.
   PubMed Web of Science ®Google Scholar
• Fersht A. (1999). Structure and mechanism in protein science: A guide to enzyme catalysis and protein folding. New York, USA: WH Freeman.
   Google Scholar
• Fuchs H, Binder R, Greischel A. (2009a). Tissue distribution of the novel DPP-4 inhibitor BI 1356 is dominated by saturable binding to its target in rats. Biopharm Drug Dispos 30:229–240.
   PubMed Web of Science ®Google Scholar
• Fuchs H, Tillement JP, Urien S, Greischel A, Roth W. (2009b). Concentration-dependent plasma protein binding of the novel dipeptidyl peptidase 4 inhibitor BI 1356 due to saturable binding to its target in plasma of mice, rats and humans. J Pharm Pharmacol 61:55–62.
   PubMed Web of Science ®Google Scholar
• Fura A, Khanna A, Vyas V, Koplowitz B, Chang SY, Caporuscio C, Boulton DW, Christopher LJ, Chadwick KD, Hamann LG, Humphreys WG, Kirby M. (2009). Pharmacokinetics of the dipeptidyl peptidase 4 inhibitor saxagliptin in rats, dogs, and monkeys and clinical projections. Drug Metab Dispos 37:1164–1171.
   PubMed Web of Science ®Google Scholar
• Greischel A, Binder R, Baierl J. (2010). The dipeptidyl peptidase-4 inhibitor linagliptin exhibits time- and dose-dependent localization in kidney, liver, and intestine after intravenous dosing: Results from high resolution autoradiography in rats. Drug Metab Dispos 38:1443–1448.
   PubMedGoogle Scholar
• Gupta R, Walunj SS, Tokala RK, Parsa KV, Singh SK, Pal M. (2009). Emerging drug candidates of dipeptidyl peptidase IV (DPP IV) inhibitor class for the treatment of Type 2 diabetes. Curr Drug Targets 10:71–87.
   PubMed Web of Science ®Google Scholar
• He H, Tran P, Yin H, Smith H, Batard Y, Wang L, Einolf H, Gu H, Mangold JB, Fischer V, Howard D. (2009a). Absorption, metabolism, and excretion of [14C]vildagliptin, a novel dipeptidyl peptidase 4 inhibitor, in humans. Drug Metab Dispos 37:536–544.
   PubMed Web of Science ®Google Scholar
• He H, Tran P, Yin H, Smith H, Flood D, Kramp R, Filipeck R, Fischer V, Howard D. (2009b). Disposition of vildagliptin, a novel dipeptidyl peptidase 4 inhibitor in rats and dogs. Drug Metab Dispos 37:545–554.
   PubMed Web of Science ®Google Scholar
• He YL, Serra D, Wang Y, Campestrini J, Riviere GJ, Deacon CF, Holst JJ, Schwartz S, Nielsen JC, Ligueros-Saylan M. (2007). Pharmacokinetics and pharmacodynamics of vildagliptin in patients with type 2 diabetes mellitus. Clin Pharmacokinet 46:577–588.
   PubMed Web of Science ®Google Scholar
• Herman GA, Stevens C, Van Dyck K, Bergman A, Yi B, De Smet M, Snyder K, Hilliard D, Tanen M, Tanaka W, Wang AQ, Zeng W, Musson D, Winchell G, Davies MJ, Ramael S, Gottesdiener KM, Wagner JA. (2005). Pharmacokinetics and pharmacodynamics of sitagliptin, an inhibitor of dipeptidyl peptidase IV, in healthy subjects: Results from two randomized, double-blind, placebo-controlled studies with single oral doses. Clin Pharmacol Ther 78:675–688.
   PubMed Web of Science ®Google Scholar
• Hughes TE, Mone MD, Russell ME, Weldon SC, Villhauer EB. (1999). NVP-DPP728 (1-[[[2-[(5-cyanopyridin-2-yl)amino]ethyl]amino]acetyl]-2-cyano-(S)- pyrrolidine), a slow-binding inhibitor of dipeptidyl peptidase IV. Biochemistry 38:11597–11603.
   PubMed Web of Science ®Google Scholar
• Kim D, Wang L, Beconi M, Eiermann GJ, Fisher MH, He H, Hickey GJ, Kowalchick JE, Leiting B, Lyons K, Marsilio F, McCann ME, Patel RA, Petrov A, Scapin G, Patel SB, Roy RS, Wu JK, Wyvratt MJ, Zhang BB, Zhu L, Thornberry NA, Weber AE. (2005). (2R)-4-oxo-4-[3-(trifluoromethyl)-5,6-dihydro[1,2,4]triazolo[4,3-a]pyrazin-7(8H)-yl]-1-(2,4,5-trifluorophenyl)butan-2-amine: A potent, orally active dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes. J Med Chem 48:141–151.
   PubMed Web of Science ®Google Scholar
• Kim YB, Kopcho LM, Kirby MS, Hamann LG, Weigelt CA, Metzler WJ, Marcinkeviciene J. (2006). Mechanism of Gly-Pro-pNA cleavage catalyzed by dipeptidyl peptidase-IV and its inhibition by saxagliptin (BMS-477118). Arch Biochem Biophys 445:9–18.
   PubMedGoogle Scholar
• Lauster CD, McKaveney TP, Muench SV. (2007). Vildagliptin: A novel oral therapy for type 2 diabetes mellitus. Am J Health Syst Pharm 64:1265–1273.
   PubMed Web of Science ®Google Scholar
• Levy G. (1994). Pharmacologic target-mediated drug disposition. Clin Pharmacol Ther 56:248–252.
   PubMed Web of Science ®Google Scholar
• Martínková L, Vejvoda V, Kren V. (2008). Selection and screening for enzymes of nitrile metabolism. J Biotechnol 133:318–326.
   PubMed Web of Science ®Google Scholar
• Matteucci E, Giampietro O. (2009). Dipeptidyl peptidase-4 (CD26): Knowing the function before inhibiting the enzyme. Curr Med Chem 16:2943–2951.
   PubMed Web of Science ®Google Scholar
• Metzler WJ, Yanchunas J, Weigelt C, Kish K, Klei HE, Xie D, Zhang Y, Corbett M, Tamura JK, He B, Hamann LG, Kirby MS, Marcinkeviciene J. (2008). Involvement of DPP-IV catalytic residues in enzyme-saxagliptin complex formation. Protein Sci 17:240–250.
   PubMed Web of Science ®Google Scholar
• Miller SA, St Onge, EL, Taylor JR. (2008). DPP-IV inhibitors: A review of sitagliptin, vildagliptin, alogliptin, and saxagliptin. Formulary 43:122–134.
   Google Scholar
• Oefner C, D’Arcy A, Mac Sweeney A, Pierau S, Gardiner R, Dale GE. (2003). High-resolution structure of human apo dipeptidyl peptidase IV/CD26 and its complex with 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl]amino)-acetyl]-2-cyano-(S)-pyrrolidine. Acta Crystallogr D Biol Crystallogr 59:1206–1212.
   PubMedGoogle Scholar
• Pei Z. (2008). From the bench to the bedside: Dipeptidyl peptidase IV inhibitors, a new class of oral antihyperglycemic agents. Curr Opin Drug Discov Devel 11:512–532.
   PubMedGoogle Scholar
• Retlich S, Duval V, Graefe-Mody U, Jaehde U, Staab A. (2010). Impact of target-mediated drug disposition on linagliptin pharmacokinetics and DPP-4 inhibition in type 2 diabetic patients. J Clin Pharmacol 50:873–885.
   PubMed Web of Science ®Google Scholar
• Retlich S, Duval V, Ring A, Staab A, Hüttner S, Jungnik A, Jaehde U, Dugi KA, Graefe-Mody U. (2010a). Pharmacokinetics and pharmacodynamics of single rising intravenous doses (0.5 mg-10 mg) and determination of absolute bioavailability of the dipeptidyl peptidase-4 inhibitor linagliptin (BI 1356) in healthy male subjects. Clin Pharmacokinet 49:829–840.
   PubMed Web of Science ®Google Scholar
• Retlich S, Withopf B, Greischel A, Staab A, Jaehde U, Fuchs H. (2009). Binding to dipeptidyl peptidase-4 determines the disposition of linagliptin (BI 1356)–investigations in DPP-4 deficient and wildtype rats. Biopharm Drug Dispos 30:422–436.
   PubMed Web of Science ®Google Scholar
• Scott LJ. (2010). Alogliptin: A review of its use in the management of type 2 diabetes mellitus. Drugs 70:2051–2072.
   PubMed Web of Science ®Google Scholar
• Tahrani AA, Piya MK, Barnett AH. (2009). Saxagliptin: A new DPP-4 inhibitor for the treatment of type 2 diabetes mellitus. Adv Ther 26:249–262.
   PubMed Web of Science ®Google Scholar
• Thomas L, Eckhardt M, Langkopf E, Tadayyon M, Himmelsbach F, Mark M. (2008). ®-8-(3-amino-piperidin-1-yl)-7-but-2-ynyl-3-methyl-1-(4-methyl-quinazolin-2-ylmethyl)-3,7-dihydro-purine-2,6-dione (BI 1356), a novel xanthine-based dipeptidyl peptidase 4 inhibitor, has a superior potency and longer duration of action compared with other dipeptidyl peptidase-4 inhibitors. J Pharmacol Exp Ther 325:175–182.
   PubMed Web of Science ®Google Scholar
• Thornberry NA, Gallwitz B. (2009). Mechanism of action of inhibitors of dipeptidyl-peptidase-4 (DPP-4). Best Pract Res Clin Endocrinol Metab 23:479–486.
   PubMed Web of Science ®Google Scholar
• Wu J, Chen Y, Shi X, Gu W. (2009). Dipeptidyl peptidase IV(DPP IV): A novel emerging target for the treatment of type 2 diabetes. J Nanjing Medical University 23:228–235.
   Google Scholar
• Zhang Z, Li Y, Stearns RA, Ortiz De Montellano PR, Baillie TA, Tang W. (2002). Cytochrome P450 3A4-mediated oxidative conversion of a cyano to an amide group in the metabolism of pinacidil. Biochemistry 41:2712–2718.
   PubMedGoogle Scholar