Insight into the correlation between lag time and aggregation rate in the kinetics of protein aggregation

Proteins: Structure, Function and Bioinformatics

Volumn 78, Issue 11, 2010, Pages 2412-2416

  Auer, Stefan ^a   Kashchiev, Dimo ^b  

^a UNIVERSITY OF LEEDS   (United Kingdom)

^b INSTITUTE OF PHYSICAL CHEMISTRY   (Bulgaria)

Author keywords

Aggregation lag time; Fraction of protein aggregated; Maximal aggregation rate; Protein aggregation diseases; Protein aggregation kinetics

Indexed keywords

ARTICLE; CORRELATION ANALYSIS; KINETICS; PARAMETER; PRIORITY JOURNAL; PROTEIN AGGREGATION; THEORY; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; PROTEIN MULTIMERIZATION; SPECTROFLUOROMETRY;

AMYLOID; PROTEIN;

AMYLOID; KINETICS; MODELS, MOLECULAR; PROTEIN MULTIMERIZATION; PROTEINS; SPECTROMETRY, FLUORESCENCE;

EID: 77955792312     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22762     Document Type: Article

References (35)

1. Sunde M, Blake C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv Protein Chem 1997; 50:123-159.
2. Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006; 75:333-366.
3. Selkoe DJ. Folding proteins in fatal ways. Nature 2003; 426:900-904.
4. Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, Thompson MJ, Balbirnie M, Wiltzius JJW, McFarlane HT, Madsen AO, Riekel C, Eisenberg D. Atomic structures of amyloid cross-β spines reveal varied steric zippers. Nature 2007; 447:453-457.
5. Tycko R. Molecular structure of amyloid fibrils: insights from solidstate NMR. Q Rev Biophys 2006; 39:1-55.
6. Hofrichter J, Ross PD, Eaton WA. Kinetics and mechanism of deoxyhemoglobin S gelation: a new approach to understanding sickle cell disease. Proc Natl Acad Sci USA 1974; 71:4864-4868.
7. Ferrone FA, Hofrichter J, Sunshine HR, Eaton WA. Kinetic studies of photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism. Biophys J 1980; 32:361-377.
8. Bishop MF, Ferrone FA. Kinetics of nucleation-controlled polymerization. Biophys J 1984; 46:631-644.
9. Ferrone FA, Hofrichter J, Eaton WA. Kinetics of sickle cell hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques. J Mol Biol 1985; 183:591-610.
10. Ferrone FA, Hofrichter J, Eaton WA. Kinetics of sickle cell hemoglobin polymerization. II. A double nucleation mechanism. J Mol Biol 1985; 183:611-631.
11. Jarrett JT, Lansbury PT. Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993; 73:1055-1058.
12. Lomakin A, Chung DS, Benedek GB, Kirschner DA, Teplow DB. On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants. Proc Natl Acad Sci USA 1996; 93:1125-1129.
13. Lomakin A, Teplow DB, Kirschner DA, Benedek GB. Kinetic theory of fibrillogenesis of amyloid β-protein. Proc Natl Acad Sci USA 1997; 94:7942-7947.
14. Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, Serpell L, Arnsdorf MF, Lindquist SL. Nucleated conformational conversion and the replication of conformational information by prion determinants. Science 2000; 289:1317-1321.
15. Galkin O, Vekilov PG. Mechanisms of homogeneous nucleation of polymers of sickle cell anemia hemoglobin in deoxy state. J Mol Biol 2004; 336:43-59.
16. Galkin O, Nagel RL, Vekilov PG. The kinetics of nucleation and growth of sickle cell hemoglobin fibers. J Mol Biol 2007; 365:425-439.
17. Auer S, Dobson CM, Vendruscolo M. Characterization of the nucleation barriers for protein aggregation and amyloid formation. HFSP J 2007; 1:137-146.
18. Auer S, Dobson C, Vendruscolo M, Maritan A. Self-templated nucleation in peptide and protein aggregation. Phys Rev Lett 2008; 101:258101.
19. Xue WF, Homans SW, Radford SE. Systematic analysis of nucleationdependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc Natl Acad Sci USA 2008; 105:8926-8931.
20. Routledge KE, Tartaglia GG, Platt GW, Vendruscolo M, Radford SE. Competition between intramolecular and intermolecular interactions in an amyloid-forming protein. J Mol Biol 2009; 389:776-786.
21. Knowles TPJ, Waudby CA, Devlin GL, Aguzzi A, Vendruscolo M, Terentjev EM, Welland ME, Dobson CM. An analytical solution to the kinetics of filament assembly. Science 2009; 326:1533-1537.
22. Zhang J, Muthukumar MJ. Simulations of nucleation and elongation of amyloid fibrils. J Chem Phys 2009; 130:035102.
23. Auer S, Kashchiev D. Phase diagram of α-helical and β-sheet forming peptides. Phys Rev Lett 2010; 104:168105.
24. Nielsen L, Khurana R, Coats A, Frokjaer S, Brange J, Vyas S, Uversky VN, Fink AL. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 2001; 40:6036-6046.
25. Kim YS, Cape SP, Chi E, Raffen R, Wilkins-Stevens P, Stevens FJ, Manning MC, Randolph TW, Solomon A, Carpenter JF. Counteracting effects of renal solutes on amyloid fibril formation by immunoglobulin light chains. J Biol Chem 2001; 276:1626-1633.
26. Zhu L, Zhang XJ, Wang LW, Zhou JM, Perret S. Relationship between stability of folding intermediates and amyloid formation for the yeast prion protein ure2p: a quantitative analysis of the effects of pH and buffer system. J Mol Biol 2003; 328:235-254.
27. Hortschansky P, Schroeckh V, Christopeit T, Zandomeneghi G, Fändrich M. The aggregation kinetics of Alzheimer's β-amyloid peptide is controlled by stochastic nucleation. Protein Sci 2005; 14:1753-1759.
28. Christopeit T, Hortschansky P, Schroeckh V, Gührs K, Zandomeneghi G, Fändrich M. Mutagenic analysis of the nucleation propensity of oxidized Alzheimer's β-amyloid peptide. Protein Sci 2005; 14:2125-2131.
29. Grudzielanek S, Smirnovas V, Winter R. Solvation-assisted pressure tuning of insulin fibrillation: from novel aggregation pathways to biotechnological applications. J Mol Biol 2006; 356:497-509.
30. Pedersen JS, Flink JM, Dikov D, Otzen D. Sulfates dramatically stabilize a salt dependent type of glucagon fibrils. Biophys J 2006; 90:4181-4194.
31. Fändrich M. Absolute correlation between lag time and growth rate in the spontaneous formation of several amyloid-like aggregates and fibrils. J Mol Biol 2007; 365:1266-1270.
32. Kashchiev D. Nucleation: basic theory with applications. Oxford: Butterworth-Heinemann; 2000.
33. Carulla N, Caddy GL, Hall DR, Zurdo J, Gairi M, Feliz M, Giralt E, Robinson CV, Dobson CM. Molecular recycling within amyloid fibrils. Nature 2005; 436:554-558.
34. Kunes KC, Cox DL, Singh RRP. One-dimensional model of yeast prion aggregation. Phys Rev E 2005; 72:051915.
35. Kashchiev D. The kinetic approach to nucleation. Cryst Res Technol 1984; 19:1413-1423.