Time evolution of amyloid fibril length distribution described by a population balance model

Chemical Engineering Science

Volumn 78, Issue , 2012, Pages 21-32

  Arosio, Paolo ^a   Beeg, Marten ^a   Nicoud, Lucrece ^a   Morbidelli, Massimo ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

lactoglobulin; Aggregation kinetics; Amyloids; Length distribution; Mathematical modeling; Population balance

Indexed keywords

AGGREGATION KINETICS; AMYLOIDS; LACTOGLOBULIN; LENGTH DISTRIBUTIONS; MATHEMATICAL MODELING; POPULATION BALANCES;

AGGLOMERATION; GLYCOPROTEINS; MOLECULAR DYNAMICS; NEURODEGENERATIVE DISEASES; NUCLEATION; POPULATION STATISTICS; STAINLESS STEEL;

KINETICS;

EID: 84861134841     PISSN: 00092509     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ces.2012.04.031     Document Type: Article

References (50)

1. Adamcik J., Jung J.M., Flakowski J., De Los Rios P., Dietler G., Mezzenga R. Understanding amyloid aggregation by statistical analysis of atomic force microscopy images. Nat. Nanotechnol. 2010, 5:423-428.
2. Akkermans C., Venema P., van der Goot A.J., Gruppen H., Bakx E.J., Boom R.M., van der Linden E. Peptides are building blocks of heat-induced fibrillar protein aggregates of beta-lactoglobulin formed at pH 2. Biomacromolecules 2008, 9:1474-1479.
3. Ako K., Nicolai T., Durand D. Salt-induced gelation of globular protein aggregates: structure and kinetics. Biomacromolecules 2010, 11:864-871.
4. Andrews J.M., Roberts C.J. A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding. J. Phys. Chem. B 2007, 111:7897-7913.
5. Arnaudov L.N., de Vries R. Theoretical modeling of the kinetics of fibrilar aggregation of bovine beta-lactoglobulin at pH 2. J. Chem. Phys. 2007, 126.
6. Arnaudov L.N., de Vries R., Ippel H., van Mierlo C.P.M. Multiple steps during the formation of beta-lactoglobulin fibrils. Biomacromolecules 2003, 4:1614-1622.
7. Bolisetty S., Adamcik J., Mezzenga R. Snapshots of fibrillation and aggregation kinetics in multistranded amyloid beta-lactoglobulin fibrils. Soft Matter 2011, 7:493-499.
8. Bromley E.H.C., Krebs M.R.H., Donald A.M. Aggregation across the length-scales in beta-lactoglobulin. Faraday Discuss. 2005, 128:13-27.
9. Carrotta R., Bauer R., Waninge R., Rischel C. Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation. Protein Sci. 2001, 10:1312-1318.
10. Chiti F., Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75:333-366.
11. Cohen S.I.A., Vendruscolo M., Welland M.E., Dobson C.M., Terentjev E.M., Knowles T.P.J. Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments. J. Chem. Phys. 2011, 135.
12. Collins S.R., Douglass A., Vale R.D., Weissman J.S. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol. 2004, 2:1582-1590.
13. Dunstan D.E., Hamilton-Brown P., Asimakis P., Ducker W., Bertolini J. Shear-induced structure and mechanics of beta-lactoglobulin amyloid fibrils. Soft Matter 2009, 5:5020-5028.
14. Ferrone F. Analysis of protein aggregation kinetics. Method Enzymol. 1999, 309:256-274.
15. Fodera V., Cataldo S., Librizzi F., Pignataro B., Spiccia P., Leone M. Self-organization pathways and spatial heterogeneity in insulin amyloid fibril formation. J. Phys. Chem. B 2009, 113:10830-10837.
16. Kardos J., Micsonai A., Pal-Gabor H., Petrik E., Graf L., Kovacs J., Lee Y.H., Naiki H., Goto Y. Reversible heat-induced dissociation of beta(2)-microglobulin amyloid fibrils. Biochemistry 2011, 50:3211-3220.
17. Knowles T.P.J., Waudby C.A., Devlin G.L., Cohen S.I.A., Aguzzi A., Vendruscolo M., Terentjev E.M., Welland M.E., Dobson C.M. An analytical solution to the kinetics of breakable filament assembly. Science 2009, 326:1533-1537.
18. Kroes-Nijboer A., Venema P., Bouman J., van der Linden E. Influence of protein hydrolysis on the growth kinetics of beta-Ig fibrils. Langmuir 2011, 27:5753-5761.
19. Kulozik U., Tolkach A., Bulca S., Hinrichs J. The role of processing and matrix design in development and control of microstructures in dairy food production - a survey. Int. Dairy J. 2003, 13:621-630.
20. Lansbury P.T., Lashuel H.A. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 2006, 443:774-779.
21. Lee C.C., Nayak A., Sethuraman A., Belfort G., McRae G.J. A three-stage kinetic model of amyloid fibrillation. Biophys. J. 2007, 92:3448-3458.
22. Lomakin, A., Chung, D.S., Benedek, G.B., Kirschner, D.A., Teplow, D.B., 1996. On the Nucleation and Growth of Amyloid beta-Protein Fibrils: Detection of Nuclei and Quantitation of Rate Constants. Proceedings of the National Academy of Sciences of the United States of America 93, 1125-1129.
23. Lomakin, A., Teplow, D.B., Kirschner, D.A., Benedek, G.B., 1997. Kinetic Theory of Fibrillogenesis of Amyloid beta-Protein. Proceedings of the National Academy of Sciences of the United States of America 94, 7942-7947.
24. 2. Int. Dairy J. 2010, 20:571-579.
25. Mahmoudi N., Mehalebi S., Nicolai T., Durand D., Riaublanc A. Light-scattering study of the structure of aggregates and gels formed by heat-denatured whey protein isolate and beta-lactoglobulin at neutral pH. J. Agric. Food. Chem. 2007, 55:3104-3111.
26. Modler A.J., Gast K., Lutsch G., Damaschun G. Assembly of amyloid protofibrils via critical oligomers - a novel pathway of amyloid formation. J. Mol. Biol. 2003, 325:135-148.
27. Morinaga A., Hasegawa K., Nomura R., Ookoshi T., Ozawa D., Goto Y., Yamada M., Naiki H. Critical role of interfaces and agitation on the nucleation of a beta amyloid fibrils at low concentrations of a beta monomers. Biochim. Biophys. Acta, Proteins Proteomics 2010, 1804:986-995.
28. Morris A.M., Watzky M.A., Finke R.G. Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature. Biochim. Biophys. Acta, Proteins Proteomics 2009, 1794:375-397.
29. Navarra G., Leone M., Militello V. Thermal aggregation of beta-lactoglobulin in presence of metal ions. Biophys. Chem. 2007, 131:52-61.
30. Nikolic A., Baud S., Rauscher S., Pomes R. Molecular mechanism of beta-sheet self-organization at water-hydrophobic interfaces. Proteins Struct. Funct. and Bioinf. 2011, 79:1-22.
31. Nilsson M.R. Techniques to study amyloid fibril formation in vitro. Methods 2004, 34:151-160.
32. Oosawa F., Kasai M. Theory of linear and helical aggregations of macromolecules. J. Mol. Biol. 1962, 4:10-21.
33. Pallitto M.M., Murphy R.M. A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state. Biophys. J. 2001, 81:1805-1822.
34. Pellarin R., Caflisch A. Interpreting the aggregation kinetics of amyloid peptides. J. Mol. Biol. 2006, 360:882-892.
35. Pellarin R., Schuetz P., Guarnera E., Caflisch A. Amyloid fibril polymorphism is under kinetic control. J. Am. Chem. Soc. 2010, 132:14960-14970.
36. Petkova A.T., Leapman R.D., Guo Z.H., Yau W.M., Mattson M.P., Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 2005, 307:262-265.
37. Powers E.T., Powers D.L. Mechanisms of protein fibril formation: nucleated polymerization with competing off-pathway aggregation. Biophys. J. 2008, 94:379-391.
38. Sasahara K., Yagi H., Sakai M., Naiki H., Goto Y. Amyloid nucleation triggered by agitation of beta(2)-microglobulin under acidic and neutral pH conditions. Biochemistry 2008, 47:2650-2660.
39. Schmit J.D., Ghosh K., Dill K. What drives amyloid molecules to assemble into oligomers and fibrils?. Biophys. J. 2011, 100:450-458.
40. Serio T.R., Cashikar A.G., Kowal A.S., Sawicki G.J., Moslehi J.J., Serpell L., Arnsdorf M.F., Lindquist S.L. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 2000, 289:1317-1321.
41. Souillac P.O., Uversky V.N., Fink A.L. Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN. Biochemistry 2003, 42:8094-8104.
42. Szymczak P., Cieplak M. Hydrodynamic effects in proteins. J. Phys. Condens. Matter 2011, 23.
43. Teoh C.L., Bekard I.B., Asimakis P., Griffin M.D.W., Ryan T.M., Dunstan D.E., Howlett G.J. Shear flow induced changes in apolipoprotein C-II Conformation and amyloid fibril formation. Biochemistry 2011, 50:4046-4057.
44. van Raaij M.E., van Gestel J., Segers-Nolten I.M.J., de Leeuw S.W., Subramaniam V. Concentration dependence of alpha-synuclein fibril length assessed by quantitative atomic force microscopy and statistical-mechanical theory. Biophys. J. 2008, 95:4871-4878.
45. Walsh D.M., Selkoe D.J. Oligomers in the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept. Lett. 2004, 11:213-228.
46. Wegner A., Savko P. Fragmentation of actin-filaments. Biochemistry 1982, 21:1909-1913.
47. Wu C., Shea J.-E. Coarse-grained models for protein aggregation. Curr. Opin. Struct. Biol. 2011, 21:209-220.
48. Xue W.F., Hellewell A.L., Gosal W.S., Homans S.W., Hewitt E.W., Radford S.E. Fibril fragmentation enhances amyloid cytotoxicity. J. Biol. Chem. 2009, 284:34272-34282.
49. Xue, W.F., Homans, S.W., Radford, S.E., 2008. Systematic Analysis of Nucleation-dependent Polymerization Reveals New Insights into the Mechanism of Amyloid Self-assembly. Proceedings of the National Academy of Sciences of the United States of America 105, 8926-8931.
50. Xue W.F., Homans S.W., Radford S.E. Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis. Protein Engineering Design & Selection 2009, 22:489-496.