Agitation of amyloid proteins to speed aggregation measured by ThT fluorescence: A call for standardization

Materials Science and Engineering C

Volumn 48, Issue , 2015, Pages 359-364

  Batzli, Kiersten M ^a   Love, Brian J ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

Author keywords

Aggregation; Agitation; Kinetics; Sigmoidal modeling; Thioflavin T fluorescence

Indexed keywords

AGGLOMERATION; AGGREGATES; ENZYME KINETICS; FLUORESCENCE; GLYCOPROTEINS; STANDARDIZATION;

AGITATION; DENATURING CONDITIONS; ELEVATED TEMPERATURE; ENVIRONMENTAL PARAMETER; EXPERIMENTAL PROCEDURE; EXPERIMENTAL PROTOCOLS; SIGMOIDAL MODEL; THIOFLAVIN T;

PROTEINS;

AMYLOID; PROTEIN AGGREGATE; THIAZOLE DERIVATIVE; THIOFLAVINE;

CHEMISTRY; FLUORESCENCE; HUMAN; PROTEIN DENATURATION; STANDARDS;

AMYLOID; FLUORESCENCE; HUMANS; PROTEIN AGGREGATES; PROTEIN DENATURATION; THIAZOLES;

EID: 84918510381     PISSN: 09284931     EISSN: 18730191     Source Type: Journal    
DOI: 10.1016/j.msec.2014.09.015     Document Type: Review

References (49)

1. M. Bartolini, and V. Andrisano Strategies for the inhibition of protein aggregation in human diseases Chembiochem 11 8 2010 1018 1035
2. W. Wang Protein aggregation and its inhibition in biopharmaceutics Int. J. Pharm. 289 1-2 2005 1 30
3. A. Ahmad, V.N. Uversky, D. Hong, and A.L. Fink Early events in the fibrillation of monomeric insulin J. Biol. Chem. 280 52 2005 42669 42675
4. L. Nielsen, S. Frokjaer, J. Brange, V.N. Uversky, and A.L. Fink Probing the mechanism of insulin fibril formation with insulin mutants Biochemistry 40 28 2001 8397 8409
5. H. Levine Thioflavin-T interaction with synthetic Alzheimer's-disease beta-amyloid peptides - detection of amyloid aggregation in solution Protein Sci. 2 3 1993 404 410
6. S. Jha, J.M. Snell, S.R. Sheftic, S.M. Patil, S.B. Daniels, F.W. Kolling, and A.T. Alexandrescu pH dependence of amylin fibrillization Biochemistry 53 2 2014 300 310
7. S.A. Hudson, H. Ecroyd, T.W. Kee, and J.A. Carver The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds FEBS J. 276 20 2009 5960 5972
8. Y. Suzuki, J.R. Brender, K. Hartman, A. Ramamoorthy, and E.N.G. Marsh Alternative pathways of human islet amyloid polypeptide aggregation distinguished by F-19 nuclear magnetic resonance-detected kinetics of monomer consumption Biochemistry 51 41 2012 8154 8162
9. R. Khurana, C. Coleman, C. Ionescu-Zanetti, S.A. Carter, V. Krishna, R.K. Grover, R. Roy, and S. Singh Mechanism of thioflavin T binding to amyloid fibrils J. Struct. Biol. 151 3 2005 229 238
10. R. Jansen, W. Dzwolak, and R. Winter Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy Biophys. J. 88 2 2005 1344 1353
11. A.F. Miller Y. Grohens, Gelation of Misfolded Proteins Polymer-Solvent Complexes and Intercalates V vol. 222 2005 109 114
12. M. Mauro, E.F. Craparo, A. Podesta, D. Bulone, R. Carrotta, V. Martorana, G. Tiana, and P.L. San Biagio Kinetics of different processes in human insulin amyloid formation J. Mol. Biol. 366 1 2007 258 274
13. H.B. Bohidar Light scattering and viscosity study of heat aggregation of insulin Biopolymers 45 1 1998 1 8
14. A.K. Attri, C. Fernandez, and A.P. Minton pH-dependent self-association of zinc-free insulin characterized by concentration-gradient static light scattering Biophys. Chem. 148 1-3 2010 28 33
15. J. Haas, E. Vohringer-Martinez, A. Bogehold, D. Matthes, U. Hensen, A. Pelah, B. Abel, and H. Grubmuller Primary steps of pH-dependent insulin aggregation kinetics are governed by conformational flexibility Chembiochem 10 11 2009 1816 1822
16. L. Nielsen, R. Khurana, A. Coats, S. Frokjaer, J. Brange, S. Vyas, V.N. Uversky, and A.L. Fink Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism Biochemistry 40 20 2001 6036 6046
17. K.R. Domike, and A.M. Donald Thermal dependence of thermally induced protein spherulite formation and growth: kinetics of beta-lactoglobulin and insulin Biomacromolecules 8 12 2007 3930 3937
18. C. Dirix, F. Meersman, L. Smeller, and K. Heremans Unfolding and fibrillogenesis of insulin: temperature, pressure and chemistry High Press. Res. 22 3-4 2002 733 736
19. A.M. Donald Why should polymer physicists study biopolymers? J. Polym. Sci. B Polym. Phys. 45 24 2007 3257 3262
20. K.R. Domike, and A.M. Donald Kinetics of spherulite formation and growth: salt and protein concentration dependence on proteins beta-lactoglobulin and insulin Int. J. Biol. Macromol. 44 4 2009 301 310
21. A.L. Kjoniksen, K.Z. Zhu, M.A. Behrens, J.S. Pedersen, and B. Nystrom Effects of temperature and salt concentration on the structural and dynamical features in aqueous solutions of charged triblock copolymers J. Phys. Chem. B 115 10 2011 2125 2139
22. J.R. Kim, and R.M. Murphy Mechanism of accelerated assembly of beta-amyloid filaments into fibrils by KLVFFK6 Biophys. J. 86 5 2004 3194 3203
23. N.A. Bernhardt, W.M. Berhanu, and U.H.E. Hansmann Mutations and seeding of amylin fibril-like oligomers J. Phys. Chem. B 117 50 2013 16076 16085
24. J.G. Biddlecombe, G. Smith, S. Uddin, S. Mulot, D. Spencer, C. Gee, B.C. Fish, and D.G. Bracewell Factors influencing antibody stability at solid-liquid interfaces in a high shear environment Biotechnol. Prog. 25 5 2009 1499 1507
25. J. Wiesbauer, M. Cardinale, and B. Nidetzky Shaking and stirring: comparison of controlled laboratory stress conditions applied to the human growth hormone Process Biochem. 48 1 2013 33 40
26. J. Jaspe, and S.J. Hagen Do protein molecules unfold in a simple shear flow? Biophys. J. 91 9 2006 3415 3424
27. S. Kiese, A. Papppenberger, W. Friess, and H.C. Mahler Shaken, not stirred: mechanical stress testing of an IgG1 antibody J. Pharm. Sci. 97 10 2008 4347 4366
28. J.S. Bee, J.L. Stevenson, B. Mehta, J. Svitel, J. Pollastrini, R. Platz, E. Freund, J.F. Carpenter, and T.W. Randolph Response of a concentrated monoclonal antibody formulation to high shear Biotechnol. Bioeng. 103 5 2009 936 943
29. C.R. Thomas, and D. Geer Effects of shear on proteins in solution Biotechnol. Lett. 33 3 2011 443 456
30. E.K. Hill, B. Krebs, D.G. Goodall, G.J. Howlett, and D.E. Dunstan Shear flow induces amyloid fibril formation Biomacromolecules 7 1 2006 10 13
31. D.E. Dunstan, P. Hamilton-Brown, P. Asimakis, W. Ducker, and J. Bertolini Shear-induced structure and mechanics of beta-lactoglobulin amyloid fibrils Soft Matter 5 24 2009 5020 5028
32. P. Hamilton-Brown, I. Bekard, W.A. Ducker, and D.E. Dunstan How does shear affect a beta fibrillogenesis? J. Phys. Chem. B 112 51 2008 16249 16252
33. D.E. Dunstan, P. Hamilton-Brown, P. Asimakis, W. Ducker, and J. Bertolini Shear flow promotes amyloid-beta fibrilization Protein Eng. Des. Sel. 22 12 2009 741 746
34. I.B. Bekard, and D.E. Dunstan Shear-induced deformation of bovine insulin in Couette flow J. Phys. Chem. B 113 25 2009 8453 8457
35. I.B. Bekard, P. Asimakis, J. Bertolini, and D.E. Dunstan The effects of shear flow on protein structure and function Biopolymers 95 11 2011 733 745
36. V. Sluzky, J.A. Tamada, A.M. Klibanov, and R. Langer Kinetics of insulin aggregation in aqueous-solutions upon agitation in the presence of hydrophobic surfaces Proc. Natl. Acad. Sci. U. S. A. 88 21 1991 9377 9381
37. K.L. De Jong, B. Incledon, C.M. Yip, and M.R. DeFelippis Amyloid fibrils of glucagon characterized by high-resolution atomic force microscopy Biophys. J. 91 5 2006 1905 1914
38. C. Veerman, L.M.C. Sagis, P. Venema, and E. van der Linden Shear-induced aggregation and break up of fibril clusters close to the percolation concentration Rheol. Acta 44 3 2005 244 249
39. S.M. Loveday, X.L. Wang, M.A. Rao, S.G. Anema, and H. Singh beta-Lactoglobulin nanofibrils: effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril dispersions Food Hydrocoll. 27 1 2012 242 249
40. G.T. Webster, J. Dusting, S. Balabani, and E.W. Blanch Detecting the early onset of shear-induced fibril formation of insulin in situ J. Phys. Chem. B 115 11 2011 2617 2626
41. C. Akkermans, P. Venema, S.S. Rogers, A.J. van der Goot, R.M. Boom, and E. van der Linden Shear pulses nucleate fibril aggregation Food Biophys. 1 3 2006 144 150
42. M. Fandrich, and C.M. Dobson Protein folding aspects of amyloid fibril formation Amyloid-J. Protein Folding Disord. 8 2001 26-26
43. L. Ashton, J. Dusting, E. Imomoh, S. Balabani, and E.W. Blanch Shear-induced unfolding of lysozyme monitored in situ Biophys. J. 96 10 2009 4231 4236
44. N.P. Humblet-Hua, L.M.C. Sagis, and E. van der Linden Effects of flow on hen egg white lysozyme (HEWL) fibril formation: length distribution, flexibility, and kinetics J. Agric. Food Chem. 56 24 2008 11875 11882
45. P.V. Stroev, P.R. Hoskins, and W.J. Easson Distribution of wall shear rate throughout the arterial tree: a case study Atherosclerosis 191 2 2007 276 280
46. M. Manno, D. Giacomazza, J. Newman, V. Martorana, and P.L. San Biagio Amyloid gels: precocious appearance of elastic properties during the formation of an insulin fibrillar network Langmuir 26 3 2010 1424 1426
47. E. Hellstrand, B. Boland, D.M. Walsh, and S. Linse Amyloid beta-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process ACS Chem. Neurosci. 1 1 2010 13 18
48. A. Tiiman, A. Noormagi, M. Friedemann, J. Krishtal, P. Palumaa, and V. Tougu Effect of agitation on the peptide fibrillization: Alzheimer's amyloid-beta peptide 1-42 but not amylin and insulin fibrils can grow under quiescent conditions J. Pept. Sci. 19 6 2013 386 391
49. R. Scherzer-Attali, R. Shaltiel-Karyo, Y.H. Adalist, D. Segal, and E. Gazit Generic inhibition of amyloidogenic proteins by two naphthoquinone-tryptophan hybrid molecules Proteins-Struct. Funct. Bioinformatics 80 8 2012 1962 1973