Inhibition of Yersinia protein tyrosine phosphatase by phosphonate derivatives of calixarenes

Bioorganic and Medicinal Chemistry Letters

Volumn 20, Issue 2, 2010, Pages 483-487

  Vovk, Andriy I ^a   Kononets, Lyudmyla A ^a   Tanchuk, Vsevolod Yu ^a   Cherenok, Sergiy O ^b   Drapailo, Andriy B ^b   Kalchenko, Vitaly I ^b   Kukhar, Valery P ^a  

^a INSTITUTE OF BIOORGANIC CHEMISTRY AND PETROCHEMISTRY   (Ukraine)

^b INSTITUTE OF ORGANIC CHEMISTRY   (Ukraine)

Author keywords

Binding mode; Calixarene; Inhibition; Molecular docking; Phosphonic acid; Protein tyrosine phosphatase

Indexed keywords

BACTERIAL ENZYME; CALIX[4]ARENE BIS(METHYLENEBISPHOSPHONIC)ACID; CALIX[4]ARENE MONO(METHYLENEBISPHOSPHONIC)ACID; CALIX[4]ARENE TETRAKIS(METHYLENEBISPHOSPHONIC)ACID; PHOSPHONIC ACID DERIVATIVE; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; COMPETITIVE INHIBITION; COMPUTER MODEL; DRUG POTENCY; DRUG SELECTIVITY; DRUG STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INHIBITION; ENZYME KINETICS; ENZYME STRUCTURE; IN VITRO STUDY; MOLECULAR DOCKING; MOLECULAR MODEL; STRUCTURE ACTIVITY RELATION; YERSINIA;

BINDING SITES; CALIXARENES; COMPUTER SIMULATION; ENZYME INHIBITORS; KINETICS; PHOSPHONIC ACIDS; PROTEIN TYROSINE PHOSPHATASES; YERSINIA;

YERSINIA;

EID: 72249115350     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2009.11.126     Document Type: Article

References (45)

1. Guan K.L., and Dixon J.E. Science 249 (1990) 553
2. Bliska J.B., Guan K., Dixon J.E., and Falkow S. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 1187
3. Cornelis G.R. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 8778
4. Persson C., Carballeira N., Wolf-Watz H., and Fallman M. EMBO J. 16 (1997) 2307
5. Black D.S., Montagna L.G., Zitsmann S., and Bliska J.B. Mol. Microbiol. 29 (1998) 1263
6. Hamid N., Gustavsson A., Andersson K., McGee K., Persson C., Rudd C.E., and Fallman M. Microb. Pathog. 26 (1999) 231
7. Black D.S., Marie-Cardine A., Schraven B., and Bliska J.B. Cell. Microbiol. 2 (2000) 401
8. de la Puerta M.L., Trinidad A.G., del Carmen Rodríguez M., Bogetz J., Sánchez Crespo M., Mustelin T., Alonso A., and Bayón Y. PLoS One 4 (2009) e4431
9. Christie A.B. Ecol. Dis. 1 (1982) 111
10. Jayaraman K.S. Nature 371 (1994) 467
11. McGovern T.W., Christopher G.W., and Eitzen E.M. Arch. Dermatol. 135 (1999) 311
12. Inglesby T.V., Dennis D.T., Henderson D.A., Bartlett J.G., Ascher M.S., Eitzen E., Fine A.D., Friedlander A.M., Hauer J., Koerner J.F., Layton M., McDade J., Osterholm M.T., O'Toole T., Parker G., Perl T.M., Russell P.K., Schoch-Spana M., and Tonat K. J. Am. Med. Assoc. 283 (2000) 2281
13. Hawley R.J., and Eitzen Jr. E.M. Annu. Rev. Microbiol. 55 (2001) 235
14. Tautz L., Bruckner S., Sareth S., Alonso A., Bogetz J., Bottini N., Pellecchia M., and Mustelin T. J. Biol. Chem. 280 (2005) 9400
15. Vazquez J., Tautz L., Ryan J.J., Vuori K., Mustelin T., and Pellecchia M. J. Med. Chem. 50 (2007) 2137
16. Chen Y.T., and Seto C.T. J. Med. Chem. 45 (2002) 3946
17. Hu X., and Stebbins C.E. Bioorg. Med. Chem. 13 (2005) 1101
18. Xie J., and Seto C.T. Bioorg. Med. Chem. 13 (2005) 2981
19. Phan J., Lee K., Cherry S., Tropea J.E., Burke Jr. T.R., and Waugh D.S. Biochemistry 42 (2003) 13113
20. Lee K., Gao Y., Yao Z.-J., Phan J., Wu L., Liang J., Waugh D.S., Zhang Z.-Y., and Burke Jr. T.R. Bioorg. Med. Chem. Lett. 13 (2003) 2577
21. Lee K., Boovanahalli S.K., Nam K.-Y., Kang S.-U., Lee M., Phan J., Wu L., Waugh D.S., Zhang Z.-Y., No K.T., Leed J.J., and Burke Jr. T.R. Bioorg. Med. Chem. Lett. 15 (2005) 4037
22. Liu S., Zhou B., Yang H., He Y., Jiang Z.-X., Kumar S., Wu L., and Zhang Z.-Y. J. Am. Chem. Soc. 130 (2008) 8251
23. Sun J.-P., Wu L., Fedorov A.A., Almo S.C., and Zhang Z.-Y. J. Biol. Chem. 278 (2003) 33392
24. Frechette R.F., Ackerman C., Beers R., and Moore J. Bioorg. Med. Chem. Lett. 7 (1997) 2169
25. Li X., Bhandari A., Holmes C.P., and Szardenings A.K. Bioorg. Med. Chem. Lett. 14 (2004) 4301
26. Holmes C.P., Li X., Pan Y., Xu C., Bhandari A., Moody C.M., Miguel J.A., Ferla S.W., De Francisco M.N., Frederick B.T., Zhou S., Macher N., Jang L., Irvine J.D., and Grove J.R. Bioorg. Med. Chem. Lett. 18 (2008) 2719
27. Iyer S., Younker J.M., Czyryca P.G., and Hengge A.C. Bioorg. Med. Chem. Lett. 14 (2004) 5931
28. Vovk A., Kalchenko V., Cherenok S., Kukhar V., Muzychka O., and Lozynsky M. Org. Biomol. Chem. 2 (2004) 3162
29. Cherenok S., Vovk A., Muravyova I., Shivanyuk A., Kukhar V., Lipkowski J., and Kalchenko V. Org. Lett. 8 (2006) 549
30. Böhmer V. Angew. Chem., Int. Ed. 34 (1995) 713-745
31. Gutsche C.D. Calixarenes Revisited. In: Stoddart J.F. (Ed). Monographs in Supramolecular Chemistry (1998), Royal Society of Chemistry, Cambridge
32. In: Asfari Z., Böhmer V., Harrowfield J., and Vicens J. (Eds). Calixarenes 2001 (2001), Kluwer Academic, Dordrecht
33. In: Vicens J., Harrowfield J., and Baklouti L. (Eds). Calixarenes in the Nanoworld (2007), Springer, Dordrecht
34. Rodik R.V., Boyko V.I., and Kalchenko V.I. Curr. Med. Chem. 16 (2009) 1630
35. Almi M., Arduini A., Casnati A., Pochini A., and Ungaro R. Tetrahedron 45 (1989) 2177
36. Kasyan O., Swierczynski D., Drapailo A., Suwinska K., Lipkowski J., and Kalchenko V. Tetrahedron Lett. 44 (2003) 7167
37. Vovk, A. I.; Kononets, L. A.; Tanchuk, V. Y.; Drapailo, A. B.; Kalchenko, V. I.; Kukhar, V. P. J. Inclusion Phenom. Macrocycl. Chem. 2009. doi:10.1007/S10847-009-9607-9.
38. Gritsenko, P. G.; Lugovsky, E. V.; Kalchenko, V. I.; Komisarenko, S. V.; Koshel, T. A.; Cherenok, S. O. Rep. Nat. Acad. Sci. Ukraine, in press.
39. Zhang Z.-Y., Clemens J.C., Schubert H.L., Stuckey J.A., Fischer M.W.F., Hume D.M., Saper M.A., and Dixon J.E. Biol. Chem. 267 (1992) 23759
40. m value was found to be 2.5 ± 0.3 mM. The kinetics of inhibition were studied at various concentrations for each inhibitor: 1: 3 μM, 6 μM; 2: 1 μM, 2 μM, 3 μM; 3: 40 μM, 80 μM; 4: 0.2 mM, 0.4 mM, 0.6 mM; 5: 0.5 μM, 1.0 μM, 1.5 μM; 6: 0.25 μM, 0.50 μM, 0.75 μM. The inhibition constants were determined measuring initial hydrolysis rates of enzyme substrate.
41. m value of the PTPβ was estimated to be 1.0 ± 0.1 mM.
42. McMartin C., and Bohacek R.S. J. Comput. Aided Mol. Des. 11 (1997) 333
43. Stuckey J.A., Schubert H.L., Fauman E.B., Zhang Z.-Y., Dixon J.E., and Saper M.A. Nature 370 (1994) 571
44. Hu X., and Stebbins C.E. Biophys. J. 91 (2006) 948
45. Hong J., and Ham S. Tetrahedron Lett. 49 (2008) 2393