Erratum: comparison of Three Amyloid Assembly Inhibitors: The Sugar scyllo-Inositol, the Polyphenol Epigallocatechin Gallate, and the Molecular Tweezer CLR01 (ACS Chem. Neurosci. (2012) 3: 6 (451-458) DOI: 10.1021/cn200133x);Comparison of three amyloid assembly inhibitors: The sugar scyllo- inositol, the polyphenol epigallocatechin gallate, and the molecular tweezer CLR01

ACS Chemical Neuroscience

Volumn 3, Issue 6, 2012, Pages 451-458

  Sinha, Sharmistha ^a   Du, Zhenming ^c   Maiti, Panchanan ^a   Klärner, Frank Gerrit ^d   Schrader, Thomas ^d   Wang, Chunyu ^c   Bitan, Gal ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^d UNIVERSITY OF DUISBURG ESSEN   (Germany)

Author keywords

Alzheimer's disease; amyloid protein; epigallocatechin gallate; inhibitor; molecular tweezers; protein aggregation; scyllo inositol

Indexed keywords

AMYLOID BETA PROTEIN; ARGININE; CLRO1; EPIGALLOCATECHIN GALLATE; LYSINE; OLIGOMER; PROTEIN INHIBITOR; SCYLLO INOSITOL; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BETA SHEET; BINDING SITE; CELL DEATH; CELL DIFFERENTIATION; CHEMICAL STRUCTURE; CONTROLLED STUDY; IN VITRO STUDY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PHEOCHROMOCYTOMA; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN BINDING; RAT;

EID: 84862851209     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/acschemneuro.2c00481     Document Type: Erratum

References (52)

1. World Alzheimer Report 2010 (2010), http://www.alz.co.uk/ research/worldreport/.
2. Kirkitadze, M. D., Bitan, G., and Teplow, D. B. (2002) Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies. J. Neurosci. Res. 69, 567-577. (Pubitemid 34966869)
3. Selkoe, D. J. (2002) Alzheimer's disease is a synaptic failure. Science 298, 789-791.
4. Selkoe, D. J. (2008) Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior. Behav. Brain Res. 192, 106-113.
5. Patterson, K. R., Remmers, C., Fu, Y., Brooker, S., Kanaan, N. M., Vana, L., Ward, S., Reyes, J. F., Philibert, K., Glucksman, M. J., and Binder, L. I. (2011) Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease. J. Biol. Chem. 286, 23063-23076.
6. Yang, F., Lim, G. P., Begum, A. N., Ubeda, O. J., Simmons, M. R., Ambegaokar, S. S., Chen, P. P., Kayed, R., Glabe, C. G., Frautschy, S. A., and Cole, G. M. (2005) Curcumin inhibits formation of amyloid βoligomers and fibrils, binds plaques, and reduces amyloid in vivo. J. Biol. Chem. 280, 5892-5901. (Pubitemid 40280072)
7. Necula, M., Kayed, R., Milton, S., and Glabe, C. G. (2007) Small molecule inhibitors of aggregation indicate that amyloid βoligomerization and fibrillization pathways are independent and distinct. J. Biol. Chem. 282, 10311-10324. (Pubitemid 47093410)
8. Ladiwala, A. R., Lin, J. C., Bale, S. S., Marcelino-Cruz, A. M., Bhattacharya, M., Dordick, J. S., and Tessier, P. M. (2010) Resveratrol selectively remodels soluble oligomers and fibrils of amyloid Aβ into off-pathway conformers. J. Biol. Chem. 285, 24228-24237.
9. Ladiwala, A. R., Dordick, J. S., and Tessier, P. M. (2011) Aromatic Small Molecules Remodel Toxic Soluble Oligomers of Amyloid β through Three Independent Pathways. J. Biol. Chem. 286, 3209-3218.
10. Di Giovanni, S., Eleuteri, S., Paleologou, K. E., Yin, G., Zweckstetter, M., Carrupt, P. A., and Lashuel, H. A. (2010) Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of α-synuclein and β-amyloid and protect against amyloid-induced toxicity. J. Biol. Chem. 285, 14941-14954.
11. Lu, J. H., Ardah, M. T., Durairajan, S. S., Liu, L. F., Xie, L. X., Fong, W. F., Hasan, M. Y., Huang, J. D., El-Agnaf, O. M., and Li, M. (2011) Baicalein Inhibits Formation of α-Synuclein Oligomers within Living Cells and Prevents Aβ Peptide Fibrillation and Oligomerisation. ChemBioChem 12, 615-624.
12. Necula, M., Breydo, L., Milton, S., Kayed, R., van der Veer, W. E., Tone, P., and Glabe, C. G. (2007) Methylene blue inhibits amyloid Aβ oligomerization by promoting fibrillization. Biochemistry 46, 8850-8860. (Pubitemid 47208418)
13. McLaurin, J., Golomb, R., Jurewicz, A., Antel, J. P., and Fraser, P. E. (2000) Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid β peptide and inhibit Aβ-induced toxicity. J. Biol. Chem. 275, 18495-18502. (Pubitemid 30414810)
14. Rezai-Zadeh, K., Shytle, D., Sun, N., Mori, T., Hou, H., Jeanniton, D., Ehrhart, J., Townsend, K., Zeng, J., Morgan, D., Hardy, J., Town, T., and Tan, J. (2005) Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice. J. Neurosci. 25, 8807-8814. (Pubitemid 41362059)
15. Fradinger, E. A., Monien, B. H., Urbanc, B., Lomakin, A., Tan, M., Li, H., Spring, S. M., Condron, M. M., Cruz, L., Xie, C. W., Benedek, G. B., and Bitan, G. (2008) C-terminal peptides coassemble into Aβ42 oligomers and protect neurons against Aβ42-induced neurotoxicity. Proc. Natl. Acad. Sci. U.S.A. 105, 14175-14180.
16. Sinha, S., Lopes, D. H., Du, Z., Pang, E. S., Shanmugam, A., Lomakin, A., Talbiersky, P., Tennstaedt, A., McDaniel, K., Bakshi, R., Kuo, P. Y., Ehrmann, M., Benedek, G. B., Loo, J. A., Klarner, F. G., Schrader, T., Wang, C., and Bitan, G. (2011) Lysine-specific molecular tweezers are broad-spectrum inhibitors of assembly and toxicity of amyloid proteins. J. Am. Chem. Soc. 133, 16958-16969.
17. Gravitz, L. (2011) Drugs: a tangled web of targets. Nature 475, S9-11.
18. Grill, J. D., and Cummings, J. L. (2010) Current therapeutic targets for the treatment of Alzheimer's disease. Expert Rev. Neurother 10, 711-728.
19. Elan and Transition Therapeutics Announce Modifications to ELND005 Phase II Clinical Trials in Alzheimer's Disease (2009), http://newsroom.elan.com/ phoenix.zhtml?c=88326&p=irolnewsArticle&ID=1365793&highlight=.
20. A Fortune in Tea Leaves - Extract Blocks Amyloid Formation (2008), http://www.alzforum.org/new/detailprint.asp?id=1838.
21. Takashima, A. (2010) TAU aggregation is a therapeutic target for Alzheimer's disease. Curr. Alzheimer Res. 7, 665-669.
22. Attar, A., Ripoli, C., Ricardi, E., Maiti, P., Sinha, S., Liu, T., Jones, M. R., Lichti-Kaiser, K., Yang, F., Gale, G. D., Tseng, C.-H., Tan, M., Xie, C. W., Staudinger, J. L., Klärner, F.-G., Schrader, T., Frautschy, S. A., Grassi, C., and Bitan, G. (2012) Lysine-specific molecular tweezers protect neurons against Aβ-induced toxicity and lower Aβand p-tau load in a mouse model of Alzheimer's disease. Submitted for publication.
23. Fokkens, M., Schrader, T., and Klärner, F. G. (2005) A molecular tweezer for lysine and arginine. J. Am. Chem. Soc. 127, 14415-14421. (Pubitemid 41457601)
24. Petkova, A. T., Ishii, Y., Balbach, J. J., Antzutkin, O. N., Leapman, R. D., Delaglio, F., and Tycko, R. (2002) A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl. Acad. Sci. U.S.A. 99, 16742-16747. (Pubitemid 36034043)
25. Usui, K., Hulleman, J. D., Paulsson, J. F., Siegel, S. J., Powers, E. T., and Kelly, J. W. (2009) Site-specific modification of Alzheimer's peptides by cholesterol oxidation products enhances aggregation energetics and neurotoxicity. Proc. Natl. Acad. Sci. U.S.A. 106, 18563-18568.
26. Sinha, S., Lopes, D. H. L., Bitan, G. (2012) A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity. ACS Chem. Neurosci., in press.
27. Li, W., Sperry, J. B., Crowe, A., Trojanowski, J. Q., Smith, A. B. 3rd, and Lee, V. M. (2009) Inhibition of tau fibrillization by oleocanthal via reaction with the amino groups of tau. J. Neurochem. 110, 1339-1351.
28. Vana, L., Kanaan, N. M., Hakala, K., Weintraub, S. T., and Binder, L. I. (2011) Peroxynitrite-induced nitrative and oxidative modifications alter tau filament formation. Biochemistry 50, 1203-1212.
29. Cohen, T. J., Guo, J. L., Hurtado, D. E., Kwong, L. K., Mills, I. P., Trojanowski, J. Q., and Lee, V. M. (2011) The acetylation of tau inhibits its function and promotes pathological tau aggregation. Nat. Commun. 2, 252.
30. Huang, A., and Stultz, C. M. (2008) The effect of a ΔK280 mutation on the unfolded state of a microtubule-binding repeat in Tau. PLoS Comput. Biol. 4, e1000155.
31. LeVine, H. 3rd. (1999) Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309, 274-284.
32. Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489. (Pubitemid 36444329)
33. Yan, Y., and Wang, C. (2006) Aβ42 is more rigid than Aβ40 at the C terminus: implications for Aβ aggregation and toxicity. J. Mol. Biol. 364, 853-862. (Pubitemid 44765041)
34. Bitan, G., Kirkitadze, M. D., Lomakin, A., Vollers, S. S., Benedek, G. B., and Teplow, D. B. (2003) Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways. Proc. Natl. Acad. Sci. U.S.A. 100, 330-335. (Pubitemid 36078074)
35. Bitan, G., Lomakin, A., and Teplow, D. B. (2001) Amyloid β- protein oligomerization: prenucleation interactions revealed by photoinduced cross-linking of unmodified proteins. J. Biol. Chem. 276, 35176-35184.
36. (2008) Research Highlights. Chemical biology: Aggravating aggregating, Nature 451, 608-609.
37. Rishton, G. M. (2008) Aggregator compounds confound amyloid fibrillization assay. Nat. Chem. Biol. 4, 159-160.
38. Feng, B. Y., Toyama, B. H., Wille, H., Colby, D. W., Collins, S. R., May, B. C., Prusiner, S. B., Weissman, J., and Shoichet, B. K. (2008) Small-molecule aggregates inhibit amyloid polymerization. Nat. Chem. Biol. 4, 197-199. (Pubitemid 351264126)
39. Martins, I. C., Kuperstein, I., Wilkinson, H., Maes, E., Vanbrabant, M., Jonckheere, W., Van Gelder, P., Hartmann, D., D'Hooge, R., De Strooper, B., Schymkowitz, J., and Rousseau, F. (2008) Lipids revert inert Aβ amyloid fibrils to neurotoxic protofibrils that affect learning in mice. EMBO J. 27, 224-233.
40. Liu, T., and Bitan, G. (2012) Modulating self-assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases - strategies and mechanisms. ChemMedChem 7, 359-374.
41. Ehrnhoefer, D. E., Bieschke, J., Boeddrich, A., Herbst, M., Masino, L., Lurz, R., Engemann, S., Pastore, A., and Wanker, E. E. (2008) EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nat. Struct. Mol. Biol. 15, 558-566. (Pubitemid 351799141)
42. Wang, S. H., Liu, F. F., Dong, X. Y., and Sun, Y. (2010) Thermodynamic analysis of the molecular interactions between amyloid β-peptide 42 and (-)-epigallocatechin-3-gallate. J. Phys. Chem. B 114, 11576-11583.
43. Liu, F. F., Dong, X. Y., He, L., Middelberg, A. P., and Sun, Y. (2011) Molecular insight into conformational transition of amyloid β-peptide 42 inhibited by (-)-epigallocatechin-3-gallate probed by molecular simulations. J. Phys. Chem. B 115, 11879-11887.
44. Weinreb, O., Amit, T., Mandel, S., and Youdim, M. B. (2009) Neuroprotective molecular mechanisms of (-)-epigallocatechin-3- gallate: a reflective outcome of its antioxidant, iron chelating and neuritogenic properties. Genes Nutr. 4, 283-296.
45. Mandel, S. A., Amit, T., Weinreb, O., and Youdim, M. B. (2011) Understanding the broad-spectrum neuroprotective action profile of green tea polyphenols in aging and neurodegenerative diseases. J. Alzheimer's Dis. 25, 187-208.
46. Queen, B. L., and Tollefsbol, T. O. (2010) Polyphenols and aging. Curr. Aging Sci. 3, 34-42.
47. Ehrnhoefer, D. E., Duennwald, M., Markovic, P., Wacker, J. L., Engemann, S., Roark, M., Legleiter, J., Marsh, J. L., Thompson, L. M., Lindquist, S., Muchowski, P. J., and Wanker, E. E. (2006) Green tea (-)-epigallocatechin- gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models. Hum. Mol. Genet. 15, 2743-2751. (Pubitemid 44400401)
48. Meng, F., Abedini, A., Plesner, A., Verchere, C. B., and Raleigh, D. P. (2010) The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity. Biochemistry 49, 8127-8133.
49. Miyata, M., Sato, T., Kugimiya, M., Sho, M., Nakamura, T., Ikemizu, S., Chirifu, M., Mizuguchi, M., Nabeshima, Y., Suwa, Y., Morioka, H., Arimori, T., Suico, M. A., Shuto, T., Sako, Y., Momohara, M., Koga, T., Morino-Koga, S., Yamagata, Y., and Kai, H. (2010) The crystal structure of the green tea polyphenol (-)-epigallocatechin gallate-transthyretin complex reveals a novel binding site distinct from the thyroxine binding site. Biochemistry 49, 6104-6114.
50. Rahimi, F., Maiti, P., and Bitan, G. (2009) Photo-induced cross-linking of unmodified proteins (PICUP) applied to amyloidogenic peptides, J. Vis. Exp. http://www.jove.com/index/details.stp?id=1071.
51. Maiti, P., Piacentini, R., Ripoli, C., Grassi, C., and Bitan, G. (2011) Surprising toxicity and assembly behaviour of amyloid β- protein oxidized to sulfone. Biochem. J. 433, 323-332.
52. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.