Thioflavin T promotes Aβ(1-40) amyloid fibrils formation

Journal of Physical Chemistry Letters

Volumn 3, Issue 12, 2012, Pages 1596-1601

  D'Amico, Michele ^a   Di Carlo, Maria Giovanna ^a   Groenning, Minna ^b   Militello, Valeria ^a   Vetri, Valeria ^a   Leone, Maurizio ^a  

^a UNIVERSITY OF PALERMO   (Italy)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION PROCESS; ALZHEIMER'S DISEASE; AMYLOID DEPOSITS; AMYLOID FIBRIL; CYTOTOXIC AGENTS; EXPERIMENTAL DATA; FIBRIL FORMATION; FIBRILLOGENESIS; FLUORESCENT DYES; FLUORESCENT PROBES; IN-VITRO; IN-VIVO; KINETIC MEASUREMENT; THIOFLAVIN T;

EXPERIMENTS; OLIGOMERS; PEPTIDES;

GLYCOPROTEINS;

EID: 84863651269     PISSN: None     EISSN: 19487185     Source Type: Journal    
DOI: 10.1021/jz300412v     Document Type: Article

References (42)

1. Selkoe, D. J. Folding Proteins in Fatal Ways. Nature 2003, 426, 900-904.
2. Dobson, C. M. Protein Folding and Misfolding. Nature 2003, 426, 884-890.
3. Makin, O. S.; Serpell, L. C. Structures for Amyloid Fibrils. FEBS J. 2005, 272, 5950-5961.
4. Uversky, V. N. Mysterious Oligomerization of the Amyloidogenic Proteins. FEBS J. 2010, 277, 2940-2953.
5. Baldwin, A. J.; Knowles, T. P. J.; Tartaglia, G. G.; Fitzpatrick, A. W.; Devlin, G. L.; Shammas, S.; Waudby, C. A.; Mossuto, M. F.; Meehan, S.; Gras, S. L.; et al. Metastability of Native Proteins and the Phenomenon of Amyloid Formation. J. Am. Chem. Soc. 2011, 133, 14160-14163.
6. Jahn, T. R.; Parker, M. J.; Homans, S. W.; Radford, S. E. Amyloid Formation Under Physiological Conditions Proceeds via a Native-Like Folding Intermediate. Nat. Struct. Mol. Biol. 2006, 13, 195-201.
7. Platt, G. W.; Routledge, K. E.; Homans, S. W.; Radford, S. E. Fibril Growth Kinetics Reveal a Region of β2-microglobulin Important for Nucleation and Elongation of Aggregation. J. Mol. Biol. 2008, 378, 251-263.
8. Langkilde, A. E.; Vestergaard, B. Methods for Structural Characterization of Prefibrillar Intermediates and Amyloid Fibrils. FEBS Lett. 2009, 583, 2600-2609.
9. Walsh, D. M.; Klyubin, I.; Fadeeva, J. V.; Rowan, M. J.; Selkoe, D. J. Amyloid-β Oligomers: their Production, Toxicity and Therapeutic Inhibition. Biochem. Soc. Trans. 2002, 30, 552-557.
10. Gharibyan, A. L.; Zamotin, V.; Yanamandra, K.; Moskaleva, O. S.; Margulis, B. A.; Kostanyan, I. A.; Morozova-Roche, L. A. Lysozyme Amyloid Oligomers and Fibrils Induce Cellular Death via Different Apoptotic/Necrotic Pathways. J. Mol. Biol. 2007, 365, 1337-1349.
11. Bieschke, J.; et al. Small-Molecule Conversion of Toxic Oligomers to Nontoxic β-Sheet Rich Amyloid Fibrils. Nat. Chem. Biol. 2012, 8, 93-101.
12. Fändrich, M. Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity. J. Mol. Biol. 2012, 10.1016/j.jmb.2012.01.006, in press.
13. LeVine, H. Quantification of β-Sheet Amyloid Fibril Structures with Thioflavin T. Methods Enzymol. 1999, 309, 274-284.
14. Groenning, M. Binding Mode of Thioflavin T and Other Molecular Probes in the Context of Amyloid Fibrils Current Status. J. Chem. Biol. 2010, 3, 1-18.
15. Biancalana, M.; Shohei, K. Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils. Biochim. Biophys. Acta 2010, 1804, 1405-1412.
16. Krebs, M.; Bromley, E.; Donald, A. The Binding of Thioflavin-T to Amyloid Fibrils: Localisation and Implications. J. Struct. Biol. 2005, 149, 30-37.
17. Khurana, R.; Coleman, C.; Ionescu-Zanetti, C.; Carter, S. A.; Krishna, V.; Grover, R. K.; Roy, R.; Singh, S. Mechanism of Thioflavin T Binding to Amyloid Fibrils. J. Struct. Biol. 2005, 151, 229-238.
18. Groenning, M.; Olsen, L.; van de Weert, M.; Flink, J. M.; Frokjaer, S.; Jørgensen, F. S. Study on the Binding of Thioflavin T to β-Sheet-Rich and Non-β-Sheet Cavities. J. Struct. Biol. 2007, 158, 358-369.
19. Groenning, M.; Norrman, M.; Flink, J. M.; van de Weert, M.; Bukrinsky, J. T.; Schluckebier, G.; Frøkjær, S. Binding Mode of Thioflavin T in Insulin Amyloid Fibrils. J. Struct. Biol. 2007, 159, 483-497.
20. Sabatè, R.; Lascu, I.; Saupe, S. J. On the Binding of Thioflavin-T to HET-s Amyloid Fibrils Assembled at pH 2. J. Struct. Biol. 2008, 162, 387-396.
21. Wu, C.; Wang, Z.; Lei, H.; Duan, Y.; Bowers, M. T.; Shea, J.-E. The Binding of Thioflavin T and Its Neutral Analog BTA-1 to Protofibrils of the Alzheimer's Disease Aβ16-22 Peptide Probed by Molecular Dynamics Simulations. J. Mol. Biol. 2008, 384, 718-729.
22. Kitts, C. C.; Bout, D. A. V. Near-Field Scanning Optical Microscopy Measurements of Fluorescent Molecular Probes Binding to Insulin Amyloid Fibrils. J. Phys. Chem. B 2009, 113, 12090-12095.
23. Stsiapura, V. I.; Maskevich, A. A.; Tikhomirov, S. A.; Buganov, O. V. Charge Transfer Process Determines Ultrafast Excited State Deactivation of Thioflavin T in Low-Viscosity Solvents. J. Phys. Chem. A 2010, 114, 8345-8350.
24. Sulatskaya, A. I.; Turoverov, K. K.; Kuznetsova, I. M. Spectral Properties and Factors Determining High Quantum Yield of Thioflavin T Incorporated in Amyloid Fibrils. Spectroscopy 2010, 24, 169-172.
25. Alavez, S.; Vantipalli, M. C.; Zucker, D. J. S.; Klang, I. M.; Lithgow, G. J. Amyloid-Binding Compounds Maintain Protein Homeostasis During Ageing and Extend Lifespan. Nature 2011, 472, 226-229.
26. Doerr, A. A Fountain of Youth (for Worms). Nat. Methods 2011, 8, 376-378.
27. Morgado, I.; Fändrich, M. Assembly of Alzheimer's Aβ Peptide into Nanostructured Amyloid Fibrils. Curr. Opin. Colloid Interface 2011, 16, 508-514.
28. Hortschansky, P.; Schroeckh, V.; Christopeit, T.; Zandomeneghi, G.; Fändrich, M. The Aggregation Kinetic of Alzheimer's β-Amyloid Peptide is Controlled by Stochastic Nucleation. Protein Sci. 2005, 14, 1753-1759.
29. Vetri, V.; Canale, C.; Relini, A.; Librizzi, F.; Militello, V.; Gliozzi, A.; Leone, M. Amyloid Fibrils Formation and Amorphous Aggregation in Concanavalin A. Biophys. Chem. 2007, 125, 184-190.
30. Carrotta, R.; Vetri, V.; Librizzi, F.; Martorana, V.; Militello, V.; Leone, M. Amyloid Fibrils Formation of Concanavalin A at Basic pH. J. Phys. Chem. B 2011, 115, 2691-2698.
31. Vetri, V.; D'Amico, M.; Foderà, V.; Leone, M.; Ponzoni, A.; Sberveglieri, G.; Militello, V. Bovine Serum Albumin Protofibril-like Aggregates Formation: Solo But Not Simple Mechanism. Arch. Biochem. Biophys. 2011, 508, 13-24.
32. Babenko, V.; Dzwolak, W.; Thioflavin, T Forms a Nonfluorescent Complex With α-Helical Poly-L-glutamic Acid. Chem. Commun. 2011, 47, 10686-10688.
33. Librizzi, F.; Foderà, V.; Vetri, V.; Lo Presti, C.; Leone, M. Effects of Confinement on Insulin Amyloid Fibrils Formation. Eur. Biophys. J. 2007, 36, 711-715.
34. Tiana, G.; Sutto, L. Equilibrium Properties of Realistic Random Heteropolymers and their Relevance for Globular and Naturally Unfolded Proteins. Phys. Rev. E 2011, 84, 061910.
35. Wahlström, A.; Hugonin, L.; Peràlvarez-Marìn, A.; Jarvet, J.; Gräslund, A. Secondary Structure Conversions of Alzheimer's Aβ(1-40) Peptide Induced by Membrane-mimicking Detergents. FEBS J. 2008, 275, 5117-5128.
36. Horvath, I.; Weise, C. F.; Andersson, E. K.; Chorell, E.; Sellstedt, M.; Bengtsson, C.; Olofsson, A.; Hultgren, S. J.; Chapman, M.; Wolf-Watz, M.; et al. Mechanisms of Protein Oligomerization: Inhibitor of Functional Amyloids Templates α-Synuclein Fibrillation. J. Am. Chem. Soc. 2012, 134, 3439-3444.
37. Vilasi, S.; Sarcina, R.; Maritato, R.; De Simone, A.; Irace, G.; Sirangelo, I. Heparin Induces Harmless Fibril Formation in Amyloidogenic W7FW14F Apomyoglobin and Amyloid Aggregation in Wild-Type Protein In Vitro. PLoS ONE 2011, 6, e22076.
38. Grelle, G.; Otto, A.; Lorenz, M.; Frank, R. F.; Wanker, E. E.; Bieschke, J. Black Tea Theaflavins Inhibit Formation of Toxic Amyloid-β and α-Synuclein Fibrils. Biochemistry 2011, 50, 10624-10636.
39. Lashuel, H. A.; Hartley, D. M.; Balakhaneh, D.; Aggarwal, A.; Teichberg, S.; Callaway, D. J. E. New Class of Inhibitors of Amyloid-β Fibril Formation. J. Biol. Chem. 2002, 277, 42881-42890.
40. D'Amico, M.; Raccosta, S.; Cannas, M.; Martorana, V.; Manno, M. Existence of Metastable Intermediate Lysozyme Conformation Highlights the Role of Alcohols in Altering Protein Stability. J. Phys. Chem. B 2011, 115, 4078-4087.
41. Fezoui, Y.; Hartley, D.; Harper, J.; Khurana, D.; Walsh, R.; Condron, M. M.; Selkoe, D.; Lansbury, P. T. J.; Fink, A.; Teplow, D. B. An Improved Method of Preparing the Amyloid β-Protein for Fibrillogenesis and Neurotoxicity Experiments. Amyloid 2000, 7, 166-178.
42. Foderà, V.; Groenning, M.; Vetri, V.; Librizzi, F.; Spagnolo, S.; Cornett, C.; Olsen, L.; van de Weert, M.; Leone, M.; Thioflavin, T Hydroxylation at Basic pH and its Effect on Amyloid Fibril Detection. J. Phys. Chem. B 2008, 112, 15174-15181.