Following the publication of the Preliminary Communication by Rafael VC Guido et al. ‘A pharmacophore-based virtual screening approach for the discovery of Trypanosoma cruzi GAPDH inhibitors’ in the November 2013 issue of Future Medicinal Chemistry (Future Med. Chem. 5[17], 2019–2035 [2013]), it has been brought to our attention that Lipinski’s rule of five, as well as a section of the references, were incorrectly printed.
Lipinski’s rule of five should have appeared as:
“According to these rules, molecules with molecular weight greater than 500; calculated log P greater than 5; more than five hydrogen bond donors or ten hydrogen bond acceptors are likely to have low oral bioavailability.”
The references (13–43) should have appeared as:
13 Pavão F, Castilho MS, Pupo MT et al. Structure of Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase complexed with chalepin, a natural product inhibitor, at 1 A resolution. FEBS Lett. 520(1–3), 13–17 (2002).
14 Castilho MS, Pavão F, Oliva G, Ladame S, Willson M, Périé J. Evidence for the two phosphate binding sites of an analogue of the thioacyl intermediate for the Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase-catalyzed reaction, from its crystal structure. Biochemistry 42(23), 7143–7151 (2003).
15 Bressi JC, Verlinde CL, Aronov AM et al. Adenosine analogues as selective inhibitors of glyceraldehyde-3-phosphate dehydrogenase of Trypanosomatidae via structure-based drug design. J. Med. Chem. 44(13), 2080–2093 (2001).
16 Aronov AM, Verlinde CL, Hol WG, Gelb MH. Selective tight binding inhibitors of trypanosomal glyceraldehyde-3-phosphate dehydrogenase via structure-based drug design. J. Med. Chem. 41(24), 4790–4799 (1998).
17 Aronov AM, Suresh S, Buckner FS et al. Structure-based design of submicromolar, biologically active inhibitors of trypanosomatid glyceraldehyde-3-phosphate dehydrogenase. Proc. Natl Acad. Sci. USA 96(8), 4273–4278 (1999).
18 Kennedy KJ, Bressi JC, Gelb MH. A disubstituted NAD+ analogue is a nanomolar inhibitor of trypanosomal glyceraldehyde-3-phosphate dehydrogenase. Bioorg. Med. Chem. Lett. 11(2), 95–98 (2001).
19 Ladame S, Castilho MS, Silva CHTP et al. Crystal structure of Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase complexed with an analogue of 1,3-bisphospho-d-glyceric acid. Eur. J. Biochem. 270(22), 4574–4586 (2003).
20 Pereira JM, Severino RP, Vieira PC et al. Anacardic acid derivatives as inhibitors of glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi. Bioorg. Med. Chem. 16(19), 8889–8888 (2008).
21 De Marchi AA, Castilho MS, Nascimento PGB et al. New 3-piperonylcoumarins as inhibitors of glycosomal glyceraldehyde-3-phosphate dehydrogenase (gGAPDH) from Trypanosoma cruzi. Bioorg. Med. Chem. 12(18), 4823–4833 (2004).
22 Macedo EMS de, Wiggers HJ, Silva MGV, Braz-Filho R, Andricopulo AD, Montanari CA. A new bianthron glycoside as inhibitor of Trypanosoma cruzi glyceraldehyde 3-phosphate dehydrogenase activity. J. Braz. Chem. Soc. 20(5), 947–953 (2009).
23 Freitas RF, Prokopczyk IM, Zottis A et al. Discovery of novel Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase inhibitors. Bioorg. Med. Chem. 17(6), 2476–2482 (2009).
24 Guido RVC, Oliva G, Andricopulo AD. Modern drug discovery technologies: opportunities and challenges in lead discovery. Comb. Chem. High Throughput Screen 14(10), 830–839 (2011).
25 Guido RVC, Oliva G, Andricopulo AD. Structure- and ligand-based drug design approaches for neglected tropical diseases. Pure Appl. Chem. 84(9), 1857–1866 (2012).
26 Ferreira RS, Guido RV, Andricopulo AD, Oliva G. In silico screening strategies for novel inhibitors of parasitic diseases. Expert Opin. Drug Discov. 6(5), 481–489 (2011).
27 Guido RVC, Oliva G, Andricopulo AD. Virtual screening and its integration with modern drug design technologies. Curr. Med. Chem. 15(1), 37–46 (2008).
28 Postigo MP, Guido RVC, Oliva G et al. Discovery of new inhibitors of Schistosoma mansoni PNP by pharmacophore-based virtual screening. J. Chem. Inf. Model. 50(9), 1693–1705 (2010).
29 Guido RVC, Balliano TL, Andricopulo AD, Oliva G. Kinetic and crystallographic studies on glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi in complex with iodoacetate. Lett. Drug Des. Discov. 6(3), 210–214 (2009).
30 Guido RVC, Cardoso CL, Moraes MC de, Andricopulo AD, Cass QB, Oliva G. Structural insights into the molecular basis responsible for the effects of immobilization on the kinetic parameters of glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi and human. J. Braz. Chem. Soc. 21(10), 1845–1853 (2010).
31 Guido RVC, Oliva G, Montanari CA, Andricopulo AD. Structural basis for selective inhibition of trypanosomatid glyceraldehyde-3-phosphate dehydrogenase: molecular docking and 3D QSAR studies. J. Chem. Inf. Model. 48(4), 918–929 (2008).
32 Souza DH, Garratt RC, Araújo AP et al.Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: structure, catalytic mechanism and targeted inhibitor design. FEBS Lett. 424(3), 131–135 (1998).
33 Davis AM, Teague SJ, Kleywegt GJ. Application and limitations of x-ray crystallographic data in structure-based ligand and drug design. Angew. Chem. Int. Ed. Engl. 42(24), 2718–2736 (2003).
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42 McGovern SL, Helfand BT, Feng B, Shoichet BK. A specific mechanism of nonspecific inhibition. J. Med. Chem. 46(20), 4265–4272 (2003).
43 Leitão A, Andricopulo AD, Oliva G et al. Structure–activity relationships of novel inhibitors of glyceraldehyde-3-phosphate dehydrogenase. Bioorg. Med. Chem. Lett. 14(9), 2199–2204 (2004).
The updated article is available on the journal website at: http://www.tandfonline.com/doi/full/10.4155/FMC.13.166
The authors and editors of Future Medicinal Chemistry would like to sincerely apologize for any inconvenience or confusion this may have caused our readers.