Novel neuraminidase inhibitors: Identification, biological evaluation and investigations of the binding mode

Future Medicinal Chemistry

Volumn 3, Issue 4, 2011, Pages 437-450

  Kirchmair, Johannes ^a   Rollinger, Judith M ^a   Liedl, Klaus R ^a   Seidel, Nora ^b   Krumbholz, Andi ^b   Schmidtke, Michaela ^b  

^a UNIVERSITY OF INNSBRUCK   (Austria)

^b FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

1 (5 HYDROXY 2,2 DIMETHYL 2H 1 BENZOPYRAN 6 YL) 2 PHENYLETHANONE; 1,4 DICAFFEOYLQUINIC ACID; 4 ACETAMIDO 5 AMINO 3 (1 ETHYLPROPOXY) 1 CYCLOHEXENE 1 CARBOXYLIC ACID; 4' O METHYLOCHNA FLAVONE; ARTOCARPIN; FLAVONOID; KATSUMADAIN A; OSELTAMIVIR; QUERCETIN 5,7,3',4' TETRAMETHYL ETHER; SIALIDASE; SIALIDASE INHIBITOR; UNCLASSIFIED DRUG; ZANAMIVIR;

ANTIVIRAL SUSCEPTIBILITY; ARTICLE; CHEMOLUMINESCENCE; CYTOTOXICITY; DRUG BINDING; DRUG EFFICACY; DRUG IDENTIFICATION; DRUG SCREENING; ENZYME ASSAY; ENZYME INHIBITION; HUMAN; IC 50; INFLUENZA A (H1N1); MOLECULAR DOCKING; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; VIRTUAL REALITY; VIRUS ISOLATION; VIRUS RESISTANCE;

ANTIVIRAL AGENTS; BINDING SITES; COMBINATORIAL CHEMISTRY TECHNIQUES; DRUG RESISTANCE, VIRAL; ENZYME INHIBITORS; INFLUENZA A VIRUS; INFLUENZA A VIRUS, H1N1 SUBTYPE; INFLUENZA B VIRUS; MOLECULAR DYNAMICS SIMULATION; NEURAMINIDASE; OSELTAMIVIR; PROTEIN BINDING;

EID: 79953667599     PISSN: 17568919     EISSN: None     Source Type: Journal    
DOI: 10.4155/fmc.10.292     Document Type: Article

References (60)

1. Webster RG, Walker EJ. Infuenza-the world is teetering on the edge of a pandemic that could kill a large fraction of the human population. Am. Sci. 91, 122-129 (2003).
2. Smith GJ, Vijaykrishna D, Bahl J et al. Origins and evolutionary genomics of the 2009 swine-origin H1N1 infuenza A epidemic. Nature 459, 1122-1125 (2009).
3. Dawood FS, Jain S, Finelli L et al. Emergence of a novel swine-origin infuenza A (H1N1) virus in humans. N Engl. J. Med. 360, 2605-2615 (2009).
4. Das K, Aramini JM, Ma LC, Krug RM, Arnold E. Structures of infuenza A proteins and insights into antiviral drug targets. Nat. Struct. Mol. Biol. 17, 530-538 (2010).
5. Neumann G, Noda T, Kawaoka Y. Emergence and pandemic potential of swine-origin H1N1 infuenza virus. Nature 459, 931-939 (2009).
6. Gong JZ, Xu WF, Zhang J. Structure and functions of infuenza virus neuraminidase. Curr. Med. Chem. 14, 113-122 (2007). (Pubitemid 46050308)
7. von Itzstein M. The war against infuenza: discovery and development of sialidase inhibitors. Nat. Rev. Drug Discov. 6, 967-974 (2007).
8. von Itzstein M, Wu WY, Kok GB et al. Rational design of potent sialidase-based inhibitors of infuenza-virus replication. Nature 363, 418-423 (1993). (Pubitemid 23179386)
9. Goodford PJ. A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J. Med. Chem. 28, 849-857 (1985). (Pubitemid 15012490)
10. Kim CU, Lew W, Williams MA. Infuenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural ana lysis of carbocyclic sialic acid analogues with potent anti-infuenza activity. J. Am. Chem. Soc 119, 681-690 (1997). (Pubitemid 27101232)
11. Sidwell RW, Smee DF. Peramivir (BCX-1812, RWJ-270201): potential new therapy for infuenza. Expert Opin. Invest. Drugs 11, 859-869 (2002). (Pubitemid 34618818)
12. Moscona A. Drug therapy-neuraminidase inhibitors for infuenza. N Engl. J. Med. 353, 1363-1373 (2005).
13. Hayden FG. Antivirals for infuenza: historical perspectives and lessons learned. Antiviral Res. 71, 372-378 (2006). (Pubitemid 44226490)
14. Bauer K, Richter M, Wutzler P, Schmidtke M. Different neuraminidase inhibitor susceptibilities of human H1N1, H1N2, and H3N2 infuenza A viruses isolated in Germany from 2001 to 2005/2006. Antiviral Res. 82, 34-41 (2009).
15. Meijer A, Lackenby A, Hungnes O et al. Oseltamivir-resistant infuenza virus A (H1N1), Europe, 2007-2008 season. Emerg Infect. Dis. 15, 552-560 (2009).
16. Moscona A. Global transmission of oseltamivir-resistant infuenza. N Engl. J. Med. 360, 953-956 (2009).
17. Weinstock DM, Zuccotti G. The evolution of infuenza resistance and treatment. JAMA Assoc 301, 1066-1069 (2009).
18. Itoh Y, Shinya K, Kiso M et al. In vitro and in vivo characterization of new swine-origin H1N1 infuenza viruses. Nature 460, 1021-1025 (2009).
19. Baz M, Abed Y, Simon P, Hamelin ME, Boivin G. Effect of the neuraminidase mutation H274Y conferring resistance to oseltamivir on the replicative capacity and virulence of old and recent human infuenza A (H1N1) viruses. J. Infect. Dis. 201, 740-745 (2010).
20. Russell RJ, Haire LF, Stevens DJ et al. The structure of H5N1 avian infuenza neuraminidase suggests new opportunities for drug design. Nature 443, 45-49 (2006) (Pubitemid 44344043)
21. An JH, Lee DCW, Law AHY et al. A novel small-molecule inhibitor of the avian infuenza H5N1 virus determined through computational screening against the neuraminidase. J. Med. Chem. 52, 2667-2672 (2009).
22. Amaro RE, Minh DDL, Cheng LS et al. Remarkable loop fexibility in avian infuenza N1 and its implications for antiviral drug design. J. Am. Chem. Soc 129, 7764-7765 (2007). (Pubitemid 46998169)
23. Amaro RE, Cheng XL, Ivanov I, Xu D, McCammon JA. Characterizing loop dynamics and ligand recognition in human-and avian-type infuenza neuraminidases via generalized born molecular dynamics and end-point free energy calculations. J. Am. Chem. Soc 131, 4702-4709 (2009).
24. Durrant JD, McCammon JA. Potential drug-like inhibitors of group 1 infuenza neuraminidase identifed through computer-aided drug design. Comput. Biol. Chem. 34, 97-105 (2010).
25. Li Y, Zhou BC, Wang RX. Rational design of tamifu derivatives targeting at the open conformation of neuraminidase subtype 1. J. Mol. Graph. Model. 28, 203-219 (2009).
26. Park JW, Jo WH. Computational design of novel, high-affnity neuraminidase inhibitors for H5N1 avian infuenza virus. Eur. J. Med. Chem. 45, 536-541 (2010).
27. Cheng LS, Amaro RE, Xu D, Li WW, Arzberger PW, McCammon JA. Ensemble-based virtual screening reveals potential novel antiviral compounds for avian infuenza neuraminidase. J. Med. Chem. 51, 3878-3894 (2008). (Pubitemid 351956517)
28. Grienke U, Schmidtke M, Kirchmair J et al. Antiviral potential and molecular insight into neuraminidase inhibiting diarylheptanoids from Alpinia katsumadai. J. Med. Chem. 53, 778-786 (2010).
29. Milne GWA, Nicklaus MC, Driscoll JS, Wang SM, Zaharevitz D. National cancer institute drug information-system 3D database. J. Chem. Inf. Comput. Sci. 34, 1219-1224 (1994).
30. Ghose AK, Pritchett A, Crippen GM. Atomic physicochemical parameters for three dimensional structure directed quantitative structure-activity relationships III: modeling hydrophobic interactions. J. Comp. Chem. 9, 80-90 (1988).
31. Hawkins PCD, Skillman AG, Warren GL, Ellingson BA, Stahl MT Conformer generation with OMEGA: algorithm and validation using high quality structures from the protein databank and cambridge structural database. J. Chem. Inf. Model. 50, 572-584 (2010).
32. Hawkins PCD, Skillman AG, Nicholls A. Comparison of shape-matching and docking as virtual screening tools. J. Med. Chem. 50, 74-82 (2007). (Pubitemid 46105500)
33. Case DA, Cheatham TE, Darden T et al. The Amber biomolecular simulation programs. J. Comp. Chem. 26, 1668-1688 (2005). (Pubitemid 43076180)
34. Dolinsky TJ, Czodrowski P, Li H et al. PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations. Nucleic Acids Res. 35, W522-W525 (2007).
35. Dolinsky TJ, Nielsen JE, McCammon JA, Baker NA. PDB2PQR: an automated pipeline for the setup of poisson-boltzmann electrostatics calculations. Nucleic Acids Res. 32, W665-W667 (2004). (Pubitemid 38997419)
36. Humphrey W, Dalke A, Schulten K. VMD: visual molecular dynamics. J. Mol. Graphics 14, 33-38, (1996). (Pubitemid 26152973)
37. Shao JY, Tanner SW, Thompson N, Cheatham TE. Clustering molecular dynamics trajectories: 1. Characterizing the performance of different clustering algorithms. J. Chem. Theory Comput. 3, 2312-2334 (2007).
38. Jones G, Willett P, Glen RC, Leach AR, Taylor R. Development and validation of a genetic algorithm for fexible docking. J. Mol. Biol. 267, 727-748 (1997). (Pubitemid 27170693)
39. Schmidtke M, Schnittler U, Jahn B, Dahse HM, Stelzner A. A rapid assay for evaluation of antiviral activity against coxsackie virus B3, infuenza virus A, and herpes simplex virus type 1. J. Virol. Methods 95, 133-143 (2001). (Pubitemid 32493844)
40. Kirchmair J, Distinto S, Markt P et al. How to optimize shape-based virtual screening: choosing the right query and including chemical information. J. Chem. Inf. Model. 49, 678-692 (2009).
41. Hamauzu Y, Yasui H, Inno T, Kume C, Omanyuda M. Phenolic profle, antioxidant property, and anti-infuenza viral activity of chinese quince (Pseudocydonia sinensis schneid.), quince (Cydonia oblonga Mill.) and apple (Malus domestica Mill.) fruits. J. Agric Food Chem. 53, 928-934 (2005). (Pubitemid 40270378)
42. Shi, S, Huang K, Zhang Y, Zhao Y, Du Q. Purifcation and identifcation of antiviral components from laggera pterodonta by high-speed counter-current chromatography. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 859, 119-124 (2007). (Pubitemid 47626097)
43. Gil-Izquierdo A, Conesa MA, Ferreres F, Gil MI. Infuence of modifed atmosphere packaging on quality, vitamin C and phenolic content of artichokes (Cynara scolymus l.). Eur. Food Res. Technol. 215, 21-27 (2002).
44. Lin LZ, Harnly JM. Identifcation of hydroxycinnamoylquinic acids of Arnica fowers and burdock roots using a standardized LC-DAD-ESI-MS profling method. J. Agric Food Chem. 56(21), 10105-10114 (2008).
45. Bauer R, Khan IA, Wagner H. TLC and HPLC ana lysis of Echinacea pallida and E. Angustifolia roots. Planta Med. 54, 426-430 (1988).
46. Liu A-L, Liu B, Qin H-L, Lee SM, Wang Y-T, Du G-H. Anti-infuenza virus activities of favonoids from the medicinal plant Elsholtzia rugulosa. Planta Med. 74, 847-851 (2008). (Pubitemid 351991120)
47. Ryu YB, Curtis-Long MJ, Lee JW et al. Structural characteristics of favanones and favones from Cudrania tricuspidata for neuraminidase inhibition. Bioorg Med. Chem. Lett. 19, 4912-4915 (2009).
48. Ryu YB, Kim JH, Park S-J et al. Inhibition of neuraminidase activity by polyphenol compounds isolated from the roots of Glycyrrhiza uralensis. Bioorg Med. Chem. Lett. 20, 971-974 (2010).
49. Jeong HJ, Ryu YB, Park S-J et al. Neuraminidase inhibitory activities of favonols isolated from Rhodiola rosea roots and their in vitro anti-infuenza viral activities. Bioorg Med. Chem. 17, 6816-6823 (2009).
50. Nagai T, Miyaichi Y, Tomimori T, Suzuki Y, Yamada H. Inhibition of infuenza virus sialidase and anti-infuenza virus activity by plant favonoids. Chem. Pharm. Bull. 38, 1329-1332 (1990). (Pubitemid 20290829)
51. Nagai T, Miyaichi Y, Tomimori T, Yamada H. Inhibition of mouse liver sialidase by plant favonoids. Biochem. Biophys. Res. Commun. 163, 25-31 (1989). (Pubitemid 19227264)
52. Mercader AG, Pomilio AB. QSAR study of favonoids and bifavonoids as infuenza H1N1 virus neuraminidase inhibitors. Eur. J. Med. Chem. 45, 1724-1730 (2010).
53. Roschek B, Fink RC, McMichael MD, Li D, Alberte RS. Elderberry favonoids bind to and prevent H1N1 infection in vitro. Phytochemistry 70, 1255-1261 (2009).
54. Lin C.N, Lu C.M, Huang P-L. Flavonoids from Artocarpus heterophyllus. Phytochemistry 39, 1447-1451 (1995).
55. Miki K, Nagai T, Suzuki K et al. Anti-infuenza virus activity of bifavonoids. Bioorg. Med. Chem. Lett. 17, 772-775 (2007).
56. Okigawa M, Kawano N, Aqil M, Rahman W. Ochnafavone and its derivatives: a new series of difavonyl ethers from Ochna squarrosa linn. J. Chem. Soc Perkin Trans. 1, 580-583 (1976).
57. Son KH, Park JO, Chung KC et al. Flavonoids from the aerial parts of Lonicera japonica. Arch. Pharmacal. Res. 15, 365-370 (1992).
58. Hong H, Neamati N, Winslow HE et al. Identifcation of HIV-1 integrase inhibitors based on a four-point pharmacophore. Antiviral Chem. Chemother. 9, 461-472 (1998). (Pubitemid 28556661)
59. Landon MR, Amaro RE, Baron, R et al. Novel druggable hot spots in avian infuenza neuraminidase H5N1 revealed by computational solvent mapping of a reduced and representative receptor ensemble. Chem. Biol. Drug Des. 71, 106-116 (2008) (Pubitemid 351160979)
60. Durrant JD, McCammon JA. Potential drug-like inhibitors of group 1 infuenza neuraminidase identifed through computer-aided drug design. Comput. Biol. Chem. 34, 97-105 (2010).