Microcalorimetry: A powerful tool for characterizing amyloid fibril formation

American Biotechnology Laboratory

Volumn 24, Issue 2, 2006, Pages 8-12

  Frasca, Verna ^a  

^a MicroCal LLC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 33646755367     PISSN: 07493223     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (38)

1. Rochet, J.C.; Lansbury, P.T., Jr. Amyloid fibrillogenesis: themes and variations. Curr. Opin. Struct. Biol. 2000, 10, 60-8.
2. Sipe, J.D.; Cohen, A.S. Review: history of the amyloid fibril. J. Struct. Biol. 2000, 130, 88-98.
3. Serpell, L.C. Alzheimer's amyloid fibrils: structure and assembly. Biochim. Biophys. Acta 2000, 1502, 16-30.
4. Dobson, C.M. Protein folding and misfolding. Nature 2003, 426, 884-90.
5. Rochet, J.C.; Outeiro, T.F.; Conway, K.A. Interactions among alpha synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease. J. Molec. Neurosci. 2004, 23, 23-34.
6. Jackson, G.S.; Clark, A.R. Mammalian prion proteins. Curr. Opin. Struct. Biol. 2000, 10, 69-74.
7. Stefani, M.; Dobson, C.M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 2003, 81, 678-99.
8. Antzutkin, O.N.; Balbach, J.J.; Leapman, R.D.; Rizzo, N.W.; Reed, J.; Tycko, R. Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils. Proc. Natl. Acad. Sci. USA 2000, 97, 13,045-50.
9. Jansen, R.; Dzwolak, W.; Winter, R. Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy. Biophys. J. 2005, 88, 1344-53.
10. Prusiner, S.B.; Groth, D.; Serban, A.; et al. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti PrP antibodies. Proc. Natl. Acad. Sci. USA 1993, 90, 10,608-12.
11. Baskakov. I.V.; Legname, G.; Prusiner, S.B.; Cohen, F.E. Folding of prion protein to its native alpha-helical conformation is under kinetic control. J. Biol. Chem. 2001, 276, 19,687-90.
12. Baskakov, I.V.; Legname, G.; Baldwin, M.A.; Prusiner, S.B.; Cohen, F.E. Pathway complexity of prion protein assembly into amyloid. J. Biol. Chem. 2002, 276, 19,687-90.
13. Kim, Y.S.; Wall, J.S.; Meyer, J.; et al. Thermodynamic modulation of light chain amyloid fibril formation. J. Biol. Chem. 2000, 275, 1570-4.
14. Kim, Y.S.; Cape, S.P.; Chi, E.; et al. Counteracting effects of renal solutes on amyloid fibril formation by immunoglobulin light chains. J. Biol. Chem. 2001, 276, 1626-33.
15. Chiti, F.; Taddei, N.; Stefani, M.; Dobson, C.M.; Ramponi, G. Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation. Prot. Sci. 2001, 10, 879-86.
16. Souillac, P.O.; Uversky, V.N.; Millett, I.S.; Khurana, R.; Doniach, S.; Fink, A.L. Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH. J. Biol. Chem. 2002, 277, 12,657-65.
17. Miroy, G.J.; Lai, Z.; Lashuel, H.; Peterson, S.A.; Strang, C.; Kelly, J.W. Inhibiting transthyretin amyloid fibril formation via protein stabilization. Proc. Natl. Acad. Sci. USA 1996, 93, 15,051-6.
18. Wiseman, T.; Williston, S.; Brandts, J.F.; Lin, L.N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 1989, 179, 131-7.
19. Leavitt, S.; Freire, E. Direct measurement of protein binding energetics by isothermal titration calorimetry. Curr. Opin. Struct. Biol. 2001, 11, 560-6.
20. Weber, P.C.; Salemme, F.R. Applications of calorimetric methods to drug discovery and the study of protein interactions. Curr. Opin. Struct. Biol. 2003, 13, 115-21.
21. Ladbury, J.E. Applications of isothermal titration calorimetry in the biological sciences: Things are heating up! Biotechniques 2004, 37, 885-7.
22. Plotnikov, V.V.; Brandts, J.M.; Lin, L.N.; Brandts, J.F. A new ultrasensitive scanning calorimeter. Anal. Biochem. 1997, 250, 237-44.
23. Plotnikov, V.; Rochalski, A.; Brandts, M.; et al. An autosampling differential scanning calorimeter instrument for studying molecular interactions. Assay Drug Devel. Technol. 2002, 1, 83-90.
24. Lin, L.N.; Brandts, J.F.; Brandts, J.M.; Plotnikov, V. Determination of the volumetric properties of proteins and other solutes using pressure perturbation calorimetry. Anal. Biochem. 2002, 302, 144-60.
25. Dzwolak, W.; Ravindra, R.; Lendermann, J.; Winter, R. Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy. Biochemistry 2003, 42, 11,347-55.
26. Cooper, A.; Johnson, C.M.; Lakey, J.H.; Nollmann, M. Heat does not come in different colours: entropy-enthalpy compensation, free energy windows, quantum confinement, pressure perturbation calorimetry, solvation and the multiple causes of heat capacity effects in biomolecular interactions. Biophys. Chem. 2001, 93, 215-30.
27. Kim, Y.S.; Randolph, T.W.; Manning, M.; Stevens, F.J.; Carpenter, J.F. Congo Red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation. J. Biol. Chem. 2003, 278, 10,842-50.
28. White, J.T.; Kelly, J.W. Support for the multigenic hypothesis of amyloidosis: the binding stoichiometry of retinol-binding protein, vitamin A, and thyroid hormone influences transthyretin amyloidogenicity in vitro. Proc. Natl. Acad. Sci. USA 2001, 98, 13,019-24.
29. Kardos, J.; Yamamoto, K.; Hasegawa, K.; Naiki, H.; Goto, Y. Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry. J. Biol. Chem. 2004, 279, 55,308-14.
30. He, X.; Zhu, G.; Koelsch, G.; Rodgers, K.K.; Zhang, X.C.; Tang, J. Biochemical and structural characterization of the interaction of memapsin 2 (β-secretase) cytosolic domain with the VHS domain of GGA proteins. Biochemistry 2003, 42, 12,174-80.
31. Kornblatt, J.A.; Marchal, S.; Rezaei, H.; Balny, C. Characterization of a complex formed between human plasminogen and recombinant sheep prion: pressure and thermal sensitivity of complex formation. Cell Molec. Biol. 2004, 50, 387-96.
32. Rezaei, H.; Choiset, Y.; Debev, P.; Groschlaude, J.; Haertlé, T. Study of stability of variants of ovine prions with different susceptibilities to scrapie. J. Therm. Anal. Cal. 2003, 71, 237-47.
33. Shnyrov, V.L.; Villar, E.; Zhadan. G.G.; et al. Comparative calorimetric study of nonamyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin. Biophys. Chem. 2000, 88, 61-7.
34. Yutani, K.; Takayama, G.; Goda, S.; et al. The process of amyloid-like fibril formation by methionine aminopeptidase from a hyperthermophile, Pyrococcus furiosus. Biochemistry 2000, 39, 2769-77.
35. Martsev, S.P.; Dubnovitsky, A.P.; Vlasov, A.P.; et al. Amyloid fibril formation of the mouse V(L) domain at acidic pH. Biochemistry 2002, 41, 3389-395.
36. Rezaei, H.; Choiset, Y.; Eghiaian, F.; et al. Amyloidogenic unfolding intermediates differentiate sheep prion protein variants. J. Molec. Biol. 2002, 322, 799-814.
37. Baxa, U.; Ross, P.D.; Wickner, R.B.; Steven, A.C. The N-terminal prion domain of Ure2p converts from an unfolded to a thermally resistant conformation upon filament formation. J. Molec. Biol. 2004, 339, 259-64.
38. Cordeiro, Y.; Kraineva, J.; Ravindra, R.; et al. Hydration and packing effects on prion folding and β-sheet conversion. J. Biol. Chem. 2004, 279, 32,354-9.