Kinetic studies of protein L aggregation and disaggregation

Biophysical Chemistry

Volumn 125, Issue 2-3, 2007, Pages 350-359

  Cellmer, Troy ^a   Douma, Rutger ^a   Huebner, Ansgar ^a   Prausnitz, John ^a,b   Blanch, Harvey ^a  

^a University of California   (United States)

^b LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

Aggregation kinetics; Amyloid; Fibrils; Protein aggregation

Indexed keywords

AMYLOID; CONGO RED; FLUOROACETIC ACID; HYDROCHLORIC ACID; MONOMER; PROTEIN; PROTEIN L; THIOFLAVINE; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL REACTION KINETICS; CONCENTRATION (PARAMETERS); FIBER; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN DETERMINATION; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEOMICS; TIME;

AMYLOIDOSIS; BACTERIAL PROTEINS; CONGO RED; DIMERIZATION; HYDROGEN-ION CONCENTRATION; KINETICS; SOLUTIONS; THIAZOLES;

EID: 33846358473     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2006.09.010     Document Type: Article

References (25)

1. Stefani M., and Dobson C.M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81 (2003) 678-699
2. Dobson C. The structural basis of protein folding and its links with human disease. Philos. Trans. R. Soc. Lond., B 356 (2001) 133-145
3. Bucciantini M., Calloni G., Chiti F., Formigli L., Nosi D., Dobson C.M., and Stefani M. Prefibrillar amyloid protein aggregates share common features of cytotoxicity. J. Biol. Chem. 279 (2004) 31374-31382
4. Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M., and Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416 (2002) 507-511
5. Petkova a.T., Leapman R.D., Guo Z.H., Yau W.M., Mattson M.P., and Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307 (2005) 262-265
6. Chiti F., Webster P., Taddei N., Clark A., Stefani M., Ramponi G., and Dobson C. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 3590-3594
7. Ramirez-Alvarado M., Merkel J.S., and Regan L. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 8979-8984
8. Zurdo J., Guijarro J.I., Jimenez J.L., Saibil H.R., and Dobson C.M. Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain. J. Mol. Biol. 311 (2001) 325-340
9. Hamada D., and Dobson C.M. A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea. Protein Sci. 11 (2002) 2417-2426
10. Fink A. Protein aggregation: folding aggregates, inclusion bodies, and amyloid. Fold. Des. 3 (1998) R9-R23
11. Goers J., Permyakov S.E., Permyakov E.A., Uversky V.N., and Fink A.L. Conformational prerequisites for alpha-lactalbumin fibrillation. Biochemistry 41 (2002) 12546-12551
12. DuBay K.F., Pawar A.P., Chiti F., Zurdo J., Dobson C.M., and Vendruscolo M. Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. J. Mol. Biol. 341 (2004) 1317-1326
13. Kim D., C.F., and Baker D. A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298 (2000) 971-984
14. Sorenson J., and Head-Gordon T. Protein engineering study of protein L by simulation. J. Comput. Biol. 9 (2002) 35-54
15. Fawzi N.L., Chubukov V., Clark L.A., Brown S., and Head-Gordon T. Influence of denatured and intermediate states of folding on protein aggregation (vol 14, pg 993, 2005). Protein Sci. 14 (2005) 1380-1380
16. Clark L.A. Protein aggregation determinants from a simplified model: cooperative folders resist aggregation. Protein Sci. 14 (2005) 653-662
17. Gu H.D., Yi Q.a., Bray S.T., Riddle D.S., Shiau a.K., and Baker D. A phage display system for studying the sequence determinants of protein-folding. Protein Sci. 4 (1995) 1108-1117
18. Ferrone F. Analysis of protein aggregation kinetics. Amyloid, Prions, and Other Protein Aggregates vol. 309 (1999) 256-274
19. Chen S.M., Ferrone F.A., and Wetzel R. Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 11884-11889
20. Ignatova Z., and Gierasch L.M. Aggregation of a slow-folding mutant of a beta-clam protein proceeds through a monomeric nucleus. Biochemistry 44 (2005) 7266-7274
21. Bishop M.F., and Ferrone F.a. Kinetics of nucleation-controlled polymerization- a perturbation treatment for use with a secondary pathway. Biophys. J. 46 (1984) 631-644
22. Hortschansky P., Schroeckh V., Christopeit T., Zandomeneghi G., and Fandrich M. The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation. Protein Sci. 14 (2005) 1753-1759
23. Hofrichter J. Kinetics of sickle hemoglobin polymerization. III. Nucleation rates determined from stochastic fluctuations in polymerization progress curves. J. Mol. Biol. 189 (1986) 553-571
24. Fawzi N.L., Chubukov V., Clark L.A., Brown S., and Head-Gordon T. Influence of denatured and intermediate states of folding on protein aggregation. Protein Sci. 14 (2005) 993-1003
25. Calamai M., Canale C., Relini A., Stefani M., Chiti F., and Dobson C.M. Reversal of protein aggregation provides evidence for multiple aggregated States. J. Mol. Biol. 346 (2005) 603-616