The kinetics of aggregation of poly-glutamic acid based polypeptides

Biophysical Chemistry

Volumn 136, Issue 2-3, 2008, Pages 74-86

  Colaco, Martin ^a   Park, Jun ^a   Blanch, Harvey ^a  

^a University of California   (United States)

Author keywords

Amyloidogenesis; Nucleated polymerization; Poly glutamic acid; Protein aggregation

Indexed keywords

ALANINE; AMYLOID; COPOLYMER; POLYGLUTAMIC ACID; POLYPEPTIDE; THIOFLAVINE;

ARTICLE; BETA SHEET; CIRCULAR DICHROISM; FLUORESCENCE; KINETICS; MOLECULAR DYNAMICS; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION;

CIRCULAR DICHROISM; COMPUTER SIMULATION; HYDROGEN-ION CONCENTRATION; KINETICS; MICROSCOPY, ATOMIC FORCE; MICROSCOPY, ELECTRON, SCANNING; MICROSCOPY, ELECTRON, TRANSMISSION; POLYGLUTAMIC ACID;

EID: 46049120228     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2008.04.008     Document Type: Article

References (32)

1. Powers E.T., and Powers D.L. The kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the "supercritical concentration". Biophys. J. 91 (2006) 122-132
2. Coluzza I., van der Vies S.M., and Frenkel D. Translocation boost protein-folding efficiency of double-barreled chaperonins. Biophys. J. 90 (2006) 3375-3381
3. Huang J.-T., and Tian J. Amino acid sequence predicts folding rate for middle-size two-state proteins. Proteins 63 (2006) 551-554
4. G. Jayachandran, V. Vishal, and V.S. Pande. 2006. Using massively parallel simulation and Markovian models to study protein folding: Examining the dynamics of the villin headpiece. J. Chem. Phys. 124:164902/164901-164902/164912.
5. Waterhouse S.H., and Gerrard J.A. Amyloid Fibrils in Bionanotechnology. Aust. J. Chem. 57 (2004) 519-523
6. Baldwin A.J., Bader R., Christodoulou J., MacPhee C.E., Dobson C.M., and Barker P.D. Cytochrome display on amyloid fibrils. J. Am. Chem. Soc. 128 (2006) 2162-2163
7. Petkova A.T., Leapman R.D., Guo Z., Yau W.-M., Mattson M.P., and Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's b-amyloid fibrils. Science 307 (2005) 262-265
8. Scheibel T. Protein fibers as performance proteins: new technologies and applications. Curr. Opin. Biotechnol. 16 (2005) 427-433
9. Scheibel T., Parthasarathy R., Sawicki G., Lin X.-M., Jaeger H., and Lindquist S.L. Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 4527-4532
10. Lamm M.S., Rajagopal K., Schneider J.P., and Pochan D.J. Laminated morphology of nontwisting b-sheet fibrils constructed via peptide self-assembly. J. Am. Chem. Soc. 127 (2005) 16692-16700
11. Schmittschmitt J.P., and Scholtz J.M. The role of protein stability, solubility, and net charge in amyloid fibril formation. Protein Sci. 12 (2003) 2374-2378
12. Nelson R., Sawaya M.R., Balbirnie M., Madsen A.O., Riekel C., Grothe R., and Eisenberg D. Structure of the cross-b spine of amyloid-like fibrils. Nature 435 (2005) 773-778
13. Brown C.L., Aksay I.A., Saville D.A., and Hecht M.H. Template-directed assembly of a de novo designed protein. J. Am. Chem. Soc. 124 (2002) 6846-6848
14. West M.W., Wang W., Patterson J., Mancias J.D., Beasley J.R., and Hecht M.H. De novo amyloid proteins from designed combinatorial libraries. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 11211-11216
15. Manno M., Craparo E.F., Martorana V., Bulone D., and San Biagio P.L. Kinetics of insulin aggregation: disentanglement of amyloid fibrillation from large-size cluster formation. Biophys. J. 90 (2006) 4585-4591
16. Cellmer T., Douma R., Huebner A., Prausnitz J., and Blanch H. Kinetic studies of protein L aggregation and disaggregation. Biophys. Chemist. 125 (2007) 350-359
17. Munishkina L.A., Henriques J., Uversky V.N., and Fink A.L. Role of protein-water interactions and electrostatics in alpha-synuclein fibril formation. Biochemistry 43 (2004) 3289-3300
18. Fawzi N.L., Okabe Y., Yap E.H., and Head-Gordon T. Determining the critical nucleus and mechanism of fibril elongation of the Alzheimer's A beta(1-40) peptide. J. Mol. Biol. 365 (2007) 535-550
19. Nguyen H.D., and Hall C.K. Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 16180-16185
20. Kodaka M. Interpretation of concentration-dependence in aggregation kinetics. Biophys. Chemist. 109 (2004) 325-332
21. Naiki H., and Gejyo F. Kinetic analysis of amyloid fibril formation. Amyloid, Prions, and Other Protein Aggregates (1999) 305-318
22. Fandrich M., and Dobson C.M. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J. 21 (2002) 5682-5690
23. MacPhee C.E., and Dobson C.M. Formation of mixed fibrils demonstrates the generic nature and potential utility of amyloid nanostructures. J. Am. Chem. Soc. 122 (2000) 12707-12713
24. Keith H.D., Giannoni G., and Padden F.J. Single Crystals of Poly(L-Glutamic Acid). Biopolymers 7 (1969) (775-&)
25. Keith H.D., Padden Jr. F.J., and Giannoni G. Crystal structures of beta-poly-L-glutamic acid and its alkaline earth salts. J. Mol. Biol. 43 (1969) 423-438
26. Krebs M.R.H., Bromley E.H.C., and Donald A.M. The binding of thioflavin-T to amyloid fibrils: localisation and implications. J. Struct. Biol. 149 (2005) 30-37
27. Bolder S.G., Sagis L.M.C., Venema P., and van der Linden E. Thioflavin T and birefringence assays to determine the conversion of proteins into fibrils. Langmuir 23 (2007) 4144-4147
28. Oosawa F., and Kasai M. Theory of linear and helical aggregations of macromolecules. J. Mol. Biol. 4 (1962) (10-&)
29. Hill T.L. Length dependence of rate constants for end-to-end association and dissociation of equilibrium linear aggregates. Biophys. J. 44 (1983) 285-288
30. Sherwood T.K., Pigford R.L., and W. C.R. Mass Transfer (1975), McGraw Hill
31. Petrescu A.J., and Receveur. Excluded volume of in the configurational distribution of a strongly denatured protein. Protein Sci. 7 (1998) 1396-1403
32. Levene P.A., and S. H.S. Calculation of isoelectric points. J. Biol. Chem. 55 (1923) 801-813