Thiosemicarbazone modification of 3-acetyl coumarin inhibits Aβ peptide aggregation and protect against Aβ-induced cytotoxicity

European Journal of Medicinal Chemistry

Volumn 121, Issue , 2016, Pages 803-809

  Ranade, Dnyanesh S ^a   Bapat, Archika M ^a   Ramteke, Shefali N ^a   Joshi, Bimba N ^a   Roussel, Pascal ^b   Tomas, Alain ^c   Deschamps, Patrick ^c   Kulkarni, Prasad P ^a  

^a AGHARKAR RESEARCH INSTITUTE   (India)

^b UNITÉ DE CATALYSE ET DE CHIMIE DU SOLIDE   (France)

^c UNIVERSITÉ PARIS DESCARTES   (France)

Author keywords

Aggregation; Alzheimer's disease; Amyloid beta peptide; Cytotoxicity; Fluorescence; Thiosemicarbazone

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; THIOSEMICARBAZONE; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); COUMARIN DERIVATIVE; NEUROPROTECTIVE AGENT; PEPTIDE FRAGMENT; PROTEIN AGGREGATE; THIOSEMICARBAZONE DERIVATIVE;

ALZHEIMER DISEASE; ARTICLE; CELL VIABILITY; COMPARATIVE STUDY; CRYSTAL STRUCTURE; CYTOTOXICITY; DRUG EFFICACY; DRUG POTENCY; DRUG SYNTHESIS; ELECTROSPRAY MASS SPECTROMETRY; HUMAN; HUMAN CELL; IC50; NEUROBLASTOMA CELL LINE; NEUROPROTECTION; PROTEIN AGGREGATION; PROTON NUCLEAR MAGNETIC RESONANCE; TURBIDITY; X RAY CRYSTALLOGRAPHY; CHEMISTRY; CONFORMATION; DRUG EFFECTS; MOLECULAR MODEL; TUMOR CELL LINE;

AMYLOID BETA-PEPTIDES; CELL LINE, TUMOR; COUMARINS; CRYSTALLOGRAPHY, X-RAY; HUMANS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; NEUROPROTECTIVE AGENTS; PEPTIDE FRAGMENTS; PROTEIN AGGREGATES; THIOSEMICARBAZONES;

EID: 84938152965     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2015.07.028     Document Type: Article

References (43)

1. [1] Holtzman, D.M., Morris, J.C., Goate, A.M., Alzheimer's disease: the challenge of the second century. Sci. Transl. Med. 3 (2011), 77–109.
2. [2] Selkoe, D.J., Folding proteins in fatal ways. Nature 426 (2003), 900–904.
3. [3] Dobson, C.M., Protein folding and misfolding. Nature 426 (2003), 884–890.
4. [4] Walsh, D.M., Klyubin, I., Fadeeva, J.V., Cullen, W.K., Anwyl, R., Wolfe, M.S., Rowan, M.J., Selkoe, D.J., Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002), 535–539.
5. [5] Seubert, P., Vigo-Pelfrey, C., Esch, F., Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids. Nature 359 (1992), 325–327.
6. [6] Hardy, J., Selkoe, D.J., The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 (2002), 353–356.
7. [7] Puchtler, H., Sweat, F., Levine, M., On the binding of congo red by amyloid. J. Histochem. Cytochem. 10 (1962), 355–364.
8. [8] Harper, J.D., Wong, S.S., Lieber, C.M., Lansbury, P.T., Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease. Biochemistry 38 (1999), 8972–8980.
9. [9] Chimon, S., Shaibat, M.A., Jones, C.R., Calero, D.C., Aizezi, B., Ishii, Y., Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid. Nat. Struct. Mol. Biol. 14 (2007), 1157–1164.
10. [10] Novitskaya, V., Bocharova, O., Bronstein, V.I., Baskakov, I.V., Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J. Biol. Chem. 281 (2006), 13828–13836.
11. [11] Haass, C., Selkoe, D.J., Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev. Mol. Cell. Biol. 8 (2007), 101–112.
12. [12] Cohena, S.I.A., Linse, S., Luheshia, L.M., Hellstrand, E., White, D., Rajaha, L., Otzenc, D.E., Vendruscoloa, M., Dobsona, C.M., Knowlesa, T.P.J., Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. PNAS 110 (2012), 9758–9763.
13. [13] Selkoe, D.J., Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior. Behav. Brain Res. 192 (2008), 106–113.
14. [14] Tomita, T., Secretase inhibitors and modulators for Alzheimer's disease treatment. Expert Rev. Neurother. 9 (2009), 661–679.
15. [15] Yatin, S.M., Yatin, M., Sridhar, V., Kenneth, B.N., Butterfield, D.A., Role of spermine in amyloid beta-peptide-associated free radical-induced neurotoxicity. J. Neurosci. Res. 63 (2001), 395–401.
16. [16] Evans, C.G., Wisen, S., Gestwicki, J.E., Heat shock proteins 70 and 90 inhibit early stages of amyloid beta (1-42) aggregation in vitro. J. Biol. Chem. 281 (2006), 33182–33191.
17. [17] Bush, A.I., Metal complexing agents as therapies for Alzheimer's disease. Neurobiol. Aging 23 (2002), 1031–1038.
18. [18] Oken, B.S., Storzbach, D.M., Kaye, J., The efficacy of Ginkgo biloba on cognitive function in Alzheimer disease. A. Arch. Neurol. 55 (1998), 1409–1415.
19. [19] Cherny, R.A., Atwood, C.S., Xilinas, M.E., Gray, D.N., Jones, W.D., McLean, C.A., Barnham, K.J., Volitakis, I., Fraser, F.W., Kim, Y.S., Huang, X.D., Goldstein, L.E., Moir, R.D., Lim, J.T., Beyreuther, K., Zheng, H., Tanzi, R.E., Masters, C.L., Bush, A.I., Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30 (2001), 665–676.
20. [20] Wang, Q., Yu, X., Patal, K., Hu, R., Chuang, S., Zhang, G., Zheng, J., Tanshinones inhibit amyloid aggregation by amyloid-β peptide, disaggregate amyloid fibrils, and protect cultured cells. ACS Chem. Neurosci. 4 (2013), 1004–1015.
21. [21] Porat, Y., Abramowitz, A., Gazit, E., Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism. Chem. Biol. Drug. Des. 67 (2006), 27–37.
22. [22] Tadamasa, A., Takushi, A., Daisuke, S., Atsuhiko, T., Takeshi, S., Youhei, S., Kanai, M., Rational design and identification of a non-peptidic aggregation inhibitor of amyloid-β based on a pharmacophore motif obtained from cyclo[-Lys-Leu-Val-Phe-Phe. Angew. Chem. Int. Ed. 53 (2014), 8236–8239.
23. [23] Riveiro, M.E., Kimpe, N.D., Moglioni, A., Vazquez, R., Monczor, F., Shayo, C., Davio, C., Coumarins: old compounds with novel promising therapeutic perspectives. Curr. Med. Chem. 17 (2010), 1325–1328.
24. [24] Anand, P., Singh, B., Singh, N., Synthesis and evaluation of novel 4-[(3H,3aH,6aH)-3-phenyl)-4,6-dioxo-2-phenyldihydro-2H-pyrrolo[3,4-d]isoxazol-5(3H,6H,6aH)-yl]benzoic acid derivatives as potent acetylcholinesterase inhibitors and anti-amnestic agents. Bioorg. Med. Chem. 20 (2012), 521–530.
25. [25] Deborah, D., Soto-Ortega, D.D., Murphy, B.P., Gonzalez–Velasuez, f.J., Wilson, K.A., Xie, F., Wang, Q., Moss, M.A., Inhibition of amyloid-b aggregation by coumarin analogs can be manipulated by functionalization of the aromatic center. Bioorg. Med. Chem. 19 (2011), 2596–2602.
26. [26] West, D., Liberta, A., Padhye, S., Chikate, R., Sonawane, P., Kumbhar, A., Yerande, R., Thiosemicarbazone complexes of copper(I1): structural and biological studies. Coord. Chem. Rev. 123 (1993), 49–71.
27. [27] Ahmad, A., Ginnebaugh, K., Li, Y., Padhye, S., Sarkar, F., Molecular targets of naturopathy in cancer research: bridge to modern medicine. Nutrients 7 (2015), 321–334.
28. [28] Padhye, S., Afrasiabi, Z., Sinn, E., Fok, J., Mehta, K., Rath, N., Antitumor metallothiosemicarbazonates: structure and antitumor activity of palladium complex of phenanthrenequinone thiosemicarbazone. Inorg. Chem. 44 (2005), 1154–1156.
29. [29] Donnelly, P., Caragounis, A., Du, T., Laughton, K., Volitakis, I., Cherny, R., Sharples, R., Hill, A., Li, Q., Masters, C.L., Barnham, K., White, A., Selective intracellular release of copper and zinc ions from bis(thiosemicarbazonato) complexes reduces levels of alzheimer disease amyloid-peptide. J. Biol. Chem. 283 (2008), 4568–4577.
30. [30] Bica, L., Liddell, J., Donnelly, P., Duncan, C., Caragounis, A., Volitakis, I., Paterson, B., Cappai, R., Grubman, A., Camakaris, J., Crouch, P., White, A., Neuroprotective copper bis(thiosemicarbazonato) complexes promote neurite elongation. PLoS One 9 (2014), 70–77.
31. [31] APEX2, Data Collection Software. 2007, Bruker AXS Inc, Madison, Wisconsin, USA mercury1.software.informer.com/3.0/.
32. [32] Bruker SAINT, 2007, Bruker AXS Inc, Madison, Wisconsin, USA.
33. [33] SADABS. 2008/1, 2007, Bruker AXS Inc., Madison, Wisconsin, USA.
34. [34] G.M. Sheldrick, SHELXS-97, Program for Crystal Structure Solution, University of Gottingen, Germany.
35. [35] Nichols, M.R., Colvin, B.A., Hood, E.A., Paranjape, G.S., Osborn, D.C., Terrill-Usery, S.E., Biophysical comparison of soluble amyloid-β(1−42) protofibrils, oligomers, and protofilaments. Biochemistry 54 (2015), 2193–2204.
36. [36] Davis, T.J., Soto-Ortega, D.D., Kotarek, J.A., Gonzalez-Velasquez, F.J., Sivakumar, K., Wu, L., Wang, Q., Moss, M.A., Comparative study of inhibition at multiple stages of amyloid-beta self-assembly provides mechanistic insight. Mol. Pharmacol. 76 (2009), 405–413.
37. [37] Dickens, M.G., Franz, K.J., A prochelator activated by hydrogen peroxide prevents metal-induced amyloid β aggregation. ChemBioChem. 11 (2010), 59–62.
38. [38] Bahramikia, S., Yazdanparast, R., Gheysarzadeh, A., Syntheses and Structure–activity relationships of seven manganese–salen derivatives as anti-amyloidogenic and fibril-destabilizing agents against hen egg-white lysozyme aggregation. Chem. Biol. Drug. Des. 80 (2012), 227–236.
39. [39] Nofal, Z.M., El-Zahar, M.I., Abdel-Karim, S.S., Novel coumarin derivatives with expected biological activity. Molecules 5 (2000), 99–113.
40. [40] Rangachari, V., Reed, D., Moore, B., Rosenberry, T., Secondary structure and interfacial aggregation of amyloid-beta (1-40) on sodium dodecyl sulfate micelles. Biochemistry 45 (2006), 8639–8648.
41. [41] Nichols, M.R., Moss, M.A., Reed, D.K., Cratic-McDaniel, S., Hoh, J.H., Rosenberry, T.L., Amyloid-beta protofibrils differ from amyloid-beta aggregates induced in dilute hexafluoroisopropanol in stability and morphology. J. Biol. Chem. 280 (2005), 2471–2480.
42. [42] Chen, W.T., Liao, Y.H., Yu, H.M., Cheng, I.H., Chen, Y.R., Distinct effects of Zn2+, Cu2+, Fe3+and Al3+on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofibril formation. J. Biol. Chem. 286 (2011), 9646–9656.
43. [43] Sharma, A.K., Pavlova, S.T., Kim, J., Finkelstein, D., Hawco, N.J., Rath, N.P., Kim, J., Mirica, L.M., Bifunctional compounds for controlling metal-mediated aggregation of the Aβ42 peptide. J. Am. Chem. Soc. 134 (2012), 6625–6636.