IJOC  Vol.2 No.4 , December 2012
Synthesis and Biological Evaluation of a Highly Constrained Analogue of Methylthioadenosine (MTA)
ABSTRACT
We describe the synthesis and the antibacterial evaluation 2’,N3-cyclonucleoside 3 analogue of MTA that is characterized by the presence of an additional linkage between the heterocyclic ring and the sugar moiety.

Cite this paper
G. Carvalho, R. Dias, J. Fourrey, V. Silva, C. Diniz and A. Silva, "Synthesis and Biological Evaluation of a Highly Constrained Analogue of Methylthioadenosine (MTA)," International Journal of Organic Chemistry, Vol. 2 No. 4, 2012, pp. 398-403. doi: 10.4236/ijoc.2012.24055.
References
[1]   E. Tacconelli, G. De Angelis, M. A. Cataldo, E. Pozzi and R. Cauda, “Does Antibiotic Exposure Increase the Risk of Methicillin-Resistant Staphylococcus Aureus (MRSA) Isolation? A Systematic Review and Meta-Analysis,” Journal of Antimicrobial Chemotherapy, Vol. 61, No. 1, 2008, pp. 26-38. doi:10.1093/jac/dkm416

[2]   D. M. Drekonja, L. M. Traynor, D. Decarolis, K. B. Crossley and J. R. Johnson, “Treatment of Non-Life-Threatening Methicillin-Resistant Staphylococcus Aureus Infections with Alternative Antimicrobial Agents: A 2-Year Retrospective Review,” Diagnostic Microbiology and Infectious Disease, Vol. 63, No. 2, 2009, pp. 201-207. doi:10.1016/j.diagmicrobio.2008.10.001

[3]   H. W. Boucher, G. H. Talbot, J. S. Bradley, J. E. Edwards Jr., D. Gilbert, L. B. Rice, M. Scheld, B. Spellberg and J. Bartlet, “Bad Bugs, No Drugs: No ESKAPE! An Update from the Infectious Diseases Society of America,” Clinical Infectious Disease, Vol. 48, No. 1, 2009, pp. 1-12. doi:10.1086/595011

[4]   M. K. Riscoe, A. J. Ferro and J. H. Fitchen, “Methionine Recycling as a Target for Antiprotozoal Drug Development,” Parasitology Today, Vol. 5, No. 10, 1989, pp. 330-333. doi:10.1016/0169-4758(89)90128-2

[5]   M. P. Barrett, J. C. Mottram and G. H. Coombs, “Recent Advances in Identifying and Validating Drug Targets in Trypanosomes and Leishmanias,” Trends in Microbiology, Vol. 7, No. 2, 1999, pp. 82-88. doi:10.1016/S0966-842X(98)01433-4

[6]   P. A. Michels, F. Bringaud, M. Herman and V. Hannaert, “Metabolic Functions of Glycosomes in Trypanosomatids,” Biochimica et Biophysica Acta, Vol. 1763, No. 12, 2006, pp. 1463-1477. doi:10.1016/j.bbamcr.2006.08.019

[7]   J. F. Barrett, J. A. Sutcliffe and T. D. Gootz, “In Vitro Assays Used to Measure the Activity of Topoisomerases,” Antimicrobial Agents and Chemotherapy, Vol. 34, No. 1, 1990, pp. 1-7. doi:10.1128/AAC.34.1.1

[8]   M. H. El Kouni, “Potential Chemotherapeutic Targets in the Purine Metabolism of Parasites,” Pharmacolology & Therapeutics, Vol. 99, No. 3, 2003, pp. 283-309. doi:10.1016/S0163-7258(03)00071-8

[9]   S. Muller, E. Liebau, R. D. Walter and R. L. Krauth-Siegel, “Thiol-Based Redox Metabolism of Protozoan Parasites,” Trends in Parasitology, Vol. 19, No. 7, 2003, pp. 320-328. doi:10.1016/S1471-4922(03)00141-7

[10]   C. H. Miller and J. A. Duerre, “S-Ribosylhomocysteine Cleavage Enzyme from Escherichia coli,” Journal of Biological Chemistry, Vol. 243, No. 1, 1968, pp. 92-97.

[11]   W. A. M. Loenen, “S-adenosylmethionine: Jack of All Trades and Master of Everything?” Biochemical Society Transactions, Vol. 34, No. 2, 2006, pp. 330-333. doi:10.1042/BST20060330

[12]   M. Fontecave, M. Atta and E. Mulliez, “S-Adenosylmethionine: Nothing Goes to Waste,” Trends in Biochemical Science, Vol. 29, No. 5, 2004, pp. 243-249. doi:10.1016/j.tibs.2004.03.007

[13]   J. E. Lee, E. C. Settembre, K. A. Cornell, M. K. Riscoe, J. R. Sufrin, S. E. Ealick and P. L. Howell, “Structural Comparison of MTA Phosphorylase and MTA/AdoHcy Nucleosidase Explains Substrate Preferences and Identifies Regions Exploitable for Inhibitor Design,” Biochemistry, Vol. 43, No. 18, 2004, pp. 5159-5169.

[14]   M. E. Tedder, Z. Nie, S. Margosiak, S. Chu, V. A. Feher, R. Almassy, K. Appelt and K. M. Yager, “Structure-Based Design, Synthesis, and Antimicrobial Activity of Purine Derived SAH/MTA Nucleosidase Inhibitors,” Bioorganic and Medicinal Chemistry, Vol. 14, No. 12, 2004, pp. 3165-3168. doi:10.1016/j.bmcl.2004.04.006

[15]   V. Singh, G. B. Evans, D. H. Lenz, J. M. Mason, K. Clinch, S. Mee, G. F. Painter, P. C. Tyler, R. H. Furneaux, J. E. Lee, P. L. Howell and V. L. Schramm, “Femtomolar Transition State Analogue inhibitors of 5’-Methylthioadenosine/S-Adenosylhomocysteine Nucleosidase from Escherichia coli,” Journal of Biological Chemistry, Vol. 280, No. 18, 2005, pp. 18265-18273. doi:10.1074/jbc.M414472200

[16]   A. Mieczkowski, V. Roy and L. A. Agrofoglio, “Preparation of Cyclonucleosides,” Chemical Reviews, Vol. 110, No. 4, 2010, pp. 1828-1856.

[17]   A. Mieczkowski and L. A. Agrofoglio, “Potential and Perspectives of Cyclonucleosides,” Current Medicinal Chemistry, Vol. 17, No. 15, 2010, pp. 1527-1549. doi:10.2174/092986710790979962

[18]   G. S. G. de Carvalho, J.-L. Fourrey, R. H. Dodd and A. D. da Silva, “Synthesis of a 4’,4’-Spirothietane-2’,N3-cycloadenosine as a Highly Constrained Analogue of 5'-Deoxy-5'-methylthioadenosine (MTA),” Tetrahedron Letters, Vol. 50, No. 4, 2009, pp. 463-466. doi:10.1016/j.tetlet.2008.11.039

[19]   D. R. Stalons and C. Thornsberry, “Broth-Dilution Method for Determining the Antibiotic Susceptibility of Anaerobic Bacteria,” Antimicrobial Agents and Chemotherapy, Vol. 7, No. 1, 1975, pp. 15-21. doi:10.1128/AAC.7.1.15

[20]   I. Zlatev, J.-L. Vasseur and F. Morvan, “Deoxygenation of 5-O-benzoyl-1,2-isopropylidene-3-O-imidazolylthiocarbonyl-α-D-xylofuranose Using Dimethyl Phosphite: An Efficient Alternate Method towards a 3’-Deoxynucleoside Glycosyl Donor,” Tetrahedron Letters, Vol. 49, No. 20, 2008, pp. 3288-3290. doi:10.1016/j.tetlet.2008.03.079

 
 
Top