Investigating the influences of redox buffer compositions on the amyloid fibrillogenesis of hen egg-white lysozyme

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 11, 2009, Pages 1663-1672

  Wang, Steven S S ^a   Liu, Kuan Nan ^a   Wu, Chia Hung ^a   Lai, Jun Kun ^a  

^a NATIONAL TAIWAN UNIVERSITY   (Taiwan)

Author keywords

Amyloid fibril; Cysteine; Cystine; Disulfide bond; Lysozyme; Redox pair

Indexed keywords

AMYLOID; BUFFER; CYSTEINE; CYSTINE; DISULFIDE; EGG WHITE; LYSOZYME;

AMYLOID FIBRILLOGENESIS; AMYLOIDOSIS; ARTICLE; CHEMICAL COMPOSITION; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; EXPERIMENTAL STUDY; FIBER; HEN; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; REACTION ANALYSIS;

AMYLOID; ANIMALS; BUFFERS; CYSTEINE; CYSTINE; DISULFIDES; KINETICS; MICROSCOPY, ELECTRON, TRANSMISSION; MURAMIDASE; OXIDATION-REDUCTION;

EID: 70249114002     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.07.017     Document Type: Article

References (72)

1. Dobson C.M. Principles of protein folding, misfolding and aggregation. Semin. Cell Dev. Biol. 15 (2004) 3-16
2. Murphy R.M. Peptide aggregation in neurodegenerative disease. Annu. Rev. Biomed. Eng. 4 (2002) 155-174
3. Ross C.A., and Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 10 (2004) S10-S17 Suppl
4. Uversky V.N., and Fink A.L. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta 1698 (2004) 131-153
5. Lai Z., Colon W., and Kelly J.W. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry 35 (1996) 6470-6482
6. Ferrao-Gonzales A.D., Souto S.O., Silva J.L., and Foguel D. The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state. Proc. Natl. Acad. Sci. USA 97 (2000) 6445-6450
7. Sluzky V., Klibanov A.M., and Langer R. Mechanism of insulin aggregation and stabilization in agitated aqueous-solutions. Biotechnol. Bioeng. 40 (1992) 895-903
8. Beaven G.H., Gratzer W.B., and Davies H.G. Formation and structure of gels and fibrils from glucagon. Eur. J. Biochem. 11 (1969) 37-42
9. Chiti F., Webster P., Taddei N., Clark A., Stefani M., Ramponi G., and Dobson C.M. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl. Acad. Sci. USA 96 (1999) 3590-3594
10. Fandrich M., Forge V., Buder K., Kittler M., Dobson C.M., and Diekmann S. Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments. Proc. Natl. Acad. Sci. USA 100 (2003) 15463-15468
11. Kallberg Y., Gustafsson M., Persson B., Thyberg J., and Johansson J. Prediction of amyloid fibril-forming proteins. J. Biol. Chem. 276 (2001) 12945-12950
12. Ji S.R., Wu Y., and Sui S.F. Study of the correlation of secondary structure of beta-amyloid peptide (Abeta40) with the hydrophobic exposure under different conditions. Gen. Physiol. Biophys. 21 (2002) 415-427
13. Lansbury Jr. P.T. Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proc. Natl. Acad. Sci. USA 96 (1999) 3342-3344
14. Soto C. Alzheimer's and prion disease as disorders of protein conformation: implications for the design of novel therapeutic approaches. J. Mol. Med. 77 (1999) 412-418
15. 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
16. Wang S.S.S., and Good T.A. An overview of Alzheimer's disease. J. Chin. Inst. Chem. Eng. 36 (2005) 533-559
17. De Felice F.G., Vieira M.N., Saraiva L.M., Figueroa-Villar J.D., Garcia-Abreu J., Liu R., Chang L., Klein W.L., and Ferreira S.T. Targeting the neurotoxic species in Alzheimer's disease: inhibitors of Abeta oligomerization. FASEB J. 18 (2004) 1366-1372
18. D. Schuster, A. Rajendran, S.W. Hui, T. Nicotera, T. Srikrishnan, M.L. Kruzel, Protective effect of colostrinin on neuroblastoma cell survival is due to reduced aggregation of beta-amyloid, Neuropeptides 39 (2005) 419-426.
19. Wang W. Protein aggregation and its inhibition in biopharmaceutics. Int. J. Pharm. 289 (2005) 1-30
20. Oberg K., Chrunyk B.A., Wetzel R., and Fink A.L. Nativelike secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR. Biochemistry 33 (1994) 2628-2634
21. Rochet J.C., and Lansbury P.T. Amyloid fibrillogenesis: themes and variations. Curr. Opin. Struct. Biol. 10 (2000) 60-68
22. Zerovnik E. Amyloid-fibril formation - proposed mechanisms and relevance to conformational disease. Eur. J. Biochem. 269 (2002) 3362-3371
23. C.M. Dobson, Protein folding and its links with human disease, Biochem. Soc. Symp. 68 (2001) 1-26.
24. Ohnishi S., and Takano K. Amyloid fibrils from the viewpoint of protein folding. Cell. Mol. Life Sci. 61 (2004) 511-524
25. Vaney M.C., Maignan S., Ries-Kautt M., and Ducriux A. High-resolution structure (1.33 A) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission. Acta Crystallogr., D Biol. Crystallogr. 52 (1996) 505-517
26. Pepys M.B., Hawkins P.N., Booth D.R., Vigushin D.M., Tennent G.A., Soutar A.K., Totty N., Nguyen O., Blake C.C., Terry C.J., et al. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 362 (1993) 553-557
27. Nielsen L., Khurana R., Coats A., Frokjaer S., Brange J., Vyas S., Uversky V.N., and Fink A.L. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 40 (2001) 6036-6046
28. Hansen R.E., Ostergaard H., Norgaard P., and Winther J.R. Quantification of protein thiols and dithiols in the picomolar range using sodium borohydride and 4, 4'-dithiodipyridine. Anal. Biochem. 363 (2007) 77-82
29. Smith P.K., Krohn R.I., Hermanson G.T., Mallia A.K., Gartner F.H., Provenzano M.D., Fujimoto E.K., Goeke N.M., Olson B.J., and Klenk D.C. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150 (1985) 76-85
30. Arnaudov L.N., and de Vries R. Thermally induced fibrillar aggregation of hen egg white lysozyme. Biophys. J. 88 (2005) 515-526
31. Nilsson M.R. Techniques to study amyloid fibril formation in vitro. Methods 34 (2004) 151-160
32. Khurana R., Gillespie J.R., Talapatra A., Minert L.J., Ionescu-Zanetti C., Millett I., and Fink A.L. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry 40 (2001) 3525-3535
33. Shashilov V.A., and Lednev I.K. 2D correlation deep UV resonance Raman spectroscopy of early events of lysozyme fibrillation: kinetic mechanism and potential interpretation pitfalls. J. Am. Chem. Soc. 130 (2008) 309-317
34. Xu M., Shashilov V.A., Ermolenkov V.V., Fredriksen L., Zagorevski D., and Lednev I.K. The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transition. Protein Sci. 16 (2007) 815-832
35. Knight J.D., Hebda J.A., and Miranker A.D. Conserved and cooperative assembly of membrane-bound alpha-helical states of islet amyloid polypeptide. Biochemistry 45 (2006) 9496-9508
36. Harada A., Azakami H., and Kato A. Amyloid fibril formation of hen lysozyme depends on the instability of the C-helix (88-99). Biosci. Biotechnol. Biochem. 72 (2008) 1523-1530
37. Khurana R., Uversky V.N., Nielsen L., and Fink A.L. Is Congo red an amyloid-specific dye?. J. Biol. Chem. 276 (2001) 22715-22721
38. Khurana R., Coleman C., Ionescu-Zanetti C., Carter S.A., Krishna V., Grover R.K., Roy R., and Singh S. Mechanism of thioflavin T binding to amyloid fibrils. J. Struct. Biol. 151 (2005) 229-238
39. Nilsson M.R. Techniques to study amyloid fibril formation in vitro. Methods 34 (2004) 151-160
40. Semisotnov G.V., Rodionova N.A., Razgulyaev O.I., Uversky V.N., Gripas A.F., and Gilmanshin R.I. Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers 31 (1991) 119-128
41. Liu C.P., Li Z.Y., Huang G.C., Perrett S., and Zhou J.M. Two distinct intermediates of trigger factor are populated during guanidine denaturation. Biochimie 87 (2005) 1023-1031
42. Smoot A.L., Panda M., Brazil B.T., Buckle A.M., Fersht A.R., and Horowitz P.M. The binding of bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL. Biochemistry 40 (2001) 4484-4492
43. Sirangelo I., Bismuto E., Tavassi S., and Irace G. Apomyoglobin folding intermediates characterized by the hydrophobic fluorescent probe 8-anilino-1-naphthalene sulfonate. Biochim. Biophys. Acta 1385 (1998) 69-77
44. Rodionova N.A., Semisotnov G.V., Kutyshenko V.P., Uverskii V.N., and Bolotina I.A. Staged equilibrium of carbonic anhydrase unfolding in strong denaturants. Mol. Biol. (Mosk.) 23 (1989) 683-692
45. Beveridge T., and Arntfield S. Heat induced changes in sulphyhydryl levels in egg white. J. Dairy Sci. 12 (1979) 173-176
46. Van der Plancken I., Van Loey A., and Hendrickx M.E. Changes in sulfhydryl content of egg white proteins due to heat and pressure treatment. J. Agric. Food Chem. 53 (2005) 5726-5733
47. Glenner G.G. Amyloid deposits and amyloidosis. The beta-fibrilloses (first of two parts). N. Engl. J. Med. 302 (1980) 1283-1292
48. Glenner G.G. Amyloid deposits and amyloidosis: the beta-fibrilloses (second of two parts). N. Engl. J. Med. 302 (1980) 1333-1343
49. Kelly J.W. Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6 (1996) 11-17
50. Rudolph R., and Lilie H. In vitro folding of inclusion body proteins. FASEB J. 10 (1996) 49-56
51. Hevehan D.L., and De Bernardez Clark E. Oxidative renaturation of lysozyme at high concentrations. Biotechnol. Bioeng. 54 (1997) 221-230
52. De Bernardez Clark E., Hevehan D., Szela S., and Maachupalli-Reddy J. Oxidative renaturation of hen egg-white lysozyme. Folding vs aggregation. Biotechnol. Prog. 14 (1998) 47-54
53. Buchner J., and Rudolph R. Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Biotechnology 9 (1991) 157-162
54. De Bernardez Clark E., Schwarz E., and Rudolph R. Inhibition of aggregation side reactions during in vitro protein folding. Amyloid, Prions, and Other Protein Aggregates vol. 309 (1999) 217-236
55. De Bernardez Clark E., Hevehan D., Szela S., and Maachupalli-Reddy J. Oxidative renaturation of hen egg-white lysozyme. Folding vs aggregation. Biotechnol. Prog. 14 (1998) 47-54
56. Paik S.R., Lee D., Cho H.J., Lee E.N., and Chang C.S. Oxidized glutathione stimulated the amyloid formation of alpha-synuclein. FEBS Lett. 537 (2003) 63-67
57. Yamamoto K., Yagi H., Ozawa D., Sasahara K., Naiki H., and Goto Y. Thiol compounds inhibit the formation of amyloid fibrils by beta 2-microglobulin at neutral pH. J. Mol. Biol. 376 (2008) 258-268
58. J.L. Kice, Electrophilic and nucleophilic catalysis of scission of sulfur-sulfur bond, Acc. Chem. Res. 1 (1968) 58-64.
59. Kice J.L., and Ekman G.E. Kinetic study of acid-catalyzed disproportionation of an unsymmetrical disulfide. J. Org. Chem. 40 (1975) 711-716
60. Benesch R.E., and Benesch R. The mechanism of disulfide interchange in acid solution - role of sulfenium ions. J. Am. Chem. Soc. 80 (1958) 1666-1669
61. A.N. Glazer, E.L. Smith, Estimation of cystine plus cysteine in proteins by disulfide interchange reaction, J. Biol. Chem. 236 (1961) 416-421.
62. Ryle A.P., and Sanger F. Disulphide interchange reactions. Biochem. J. 60 (1955) 535-540
63. T.E. Isles, P.C. Jocelyn, Reaction of protein thiol groups with some disulphides, Biochem. J. 88 (1963) 84-88.
64. Kumar S., Ravi V.K., and Swaminathan R. How do surfactants and DTT affect the size, dynamics, activity and growth of soluble lysozyme aggregates?. Biochem. J. 415 (2008) 275-288
65. Bosques C.J., and Imperiali B. The interplay of glycosylation and disulfide formation influences fibrillization in a prion protein fragment. Proc. Natl. Acad. Sci. USA 100 (2003) 7593-7598
66. Ohhashi Y., Hagihara Y., Kozhukh G., Hoshino M., Hasegawa K., Yamaguchi I., Naiki H., and Goto Y. The intrachain disulfide bond of beta(2)-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH. J. Biochem. 131 (2002) 45-52
67. El-Agnaf O.M., Sheridan J.M., Sidera C., Siligardi G., Hussain R., Haris P.I., and Austen B.M. Effect of the disulfide bridge and the C-terminal extension on the oligomerization of the amyloid peptide ABri implicated in familial British dementia. Biochemistry 40 (2001) 3449-3457
68. Zhang Q.H., and Kelly J.W. Cys10 mixed disulfides make transthyretin more amyloidogenic under mildly acidic conditions. Biochemistry 42 (2003) 8756-8761
69. Das A.K., Drew M.G., Haldar D., and Banerjee A. The role of the disulfide bond in amyloid-like fibrillogenesis in a model peptide system. Org. Biomol. Chem. 3 (2005) 3502-3507
70. Thorn D.C., Ecroyd H., Sunde M., Poon S., and Carver J.A. Amyloid fibril formation by bovine milk alpha s2-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha s1-casein. Biochemistry 47 (2008) 3926-3936
71. Cao A., Hu D., and Lai L. Formation of amyloid fibrils from fully reduced hen egg white lysozyme. Protein Sci. 13 (2004) 319-324
72. Axelsson K., and Mannervik B. Synthesis of a mixed disulfide of egg white lysozyme and glutathione - a model substrate for enzymatic reduction of protein mixed disulfides. FEBS Lett. 53 (1975) 40-43