Methanol-induced tertiary and secondary structure changes of granulocyte-colony stimulating factor

Journal of Biochemistry

Volumn 140, Issue 1, 2006, Pages 49-56

  Yamazaki, Katsuyoshi ^a,b   Iwura, Takafumi ^a   Ishikawa, Rika ^a   Ozaki, Yukihiro ^b  

^a KIRIN BREWERY CO LTD   (Japan)

^b KWANSEI GAKUIN UNIVERSITY   (Japan)

Author keywords

Conformational changes; G CSF; Intermediate state

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; GRANULOCYTE COLONY STIMULATING FACTOR; METHANOL;

ARTICLE; CHEMICAL BINDING; CIRCULAR DICHROISM; DENATURATION; FLUORESCENCE SPECTROSCOPY; INFRARED SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

ANILINO NAPHTHALENESULFONATES; CIRCULAR DICHROISM; DOSE-RESPONSE RELATIONSHIP, DRUG; FILGRASTIM; HEAT; METHANOL; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, INFRARED;

EID: 33748938328     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj133     Document Type: Article

References (46)

1. Kim, P.S. and Baldwin, R.L. (1982) Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51, 459-489
2. Ptitsyn, O.B. (1987) Protein folding: hypotheses and experiments. J. Protein Chem. 6, 273-293
3. Nakao, M., Maki, K., Arai, M., Koshiba, T., Nitta, K., and Kuwajima, K. (2005) Characterization of kinetic folding intermediates of recombinant canine milk lysozyme by stopped-flow circular dichroism. Biochemistry 44, 6685-6692
4. Nakao, M., Arai, M., Koshiba, T., Nitta, K., and Kuwajima, K. (2003) Folding mechanism of canine milk lysozyme studied by circular dichroism and fluorescence spectroscopy. Spectroscopy 17, 183-193
5. Dael, H.V., Haezebrouck, P., and Joniau, M. (2003) Equilibrium and kinetic studies on folding of canine milk lysozyme. Protein Sci. 12, 609-619
6. Kuwajima, K. (1992) Protein folding in vitro. Curr. Opin. Biotechnol. 3, 462-467
7. Dobson, C.M. (1992) Unfolded proteins, compact states and molten globules. Curr. Opin. Struct. Biol. 2, 6-12
8. Ptitsyn, O.B., Pain, R.H., Semisotnov, G.V., Zerovnik, E., and Razgulyaev, O.I. (1990) Evidence for a molten globule state as a general intermediate in protein folding. FEBS Lett. 262, 20-24
9. Kuwajima, K. (1989) The molten globule as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6, 87-103
10. Christensen, H., and Pain, R.H. (1991) Molten globule intermediates and protein folding. Eur. Biophys J. 19, 221-229
11. Fink, A.L. (1995) Compact intermediate state in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24, 495-522
12. Bychkova, V.E., Dujsekina, A.E., Klenin, S.I., Tiktopulo, E.I., Uversky, V.N., and Ptitsyn, O.B. (1996) Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface. Biochemistry 35, 6058-6063
13. Uversky, V.N., Narizhneva, N.V., Kirschstein, S.O., Winter, S., and Löber, G. (1997) Conformational transitions provoked by organic solvents in β-lactoglobulin: can a molten globule like intermediate be induced by the decrease in dielectric constant? Folding Design 2, 163-172
14. Babu, K.R. and Douglas, D.J. (2000) Methanol-induced conformations of myoglobin at pH 4.0. Biochemistry 39, 14702-14710
15. Alexandrescu, A.T., Ng, Y., and Dobson, C.M. (1994) Characterization of a trifluoroethanol-induced partially folded state of α-lactalbumin. J. Mol. Biol. 235, 587-599
16. Kamatari, Y.O., Konno, T., Kataoka, M., and Akasaka, K. (1996) The methanol-induced globular and expanded denatured states of cytochrome c: a study by CD, fluorescence, NMR and small-angle X-ray scattering. J. Mol. Biol. 259, 512-523
17. Shiraki, K., Nishikawa, K., and Goto, Y. (1995) Trifluoroethanol-induced stabilization of α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245, 180-194
18. Buck, M., Radford, S.E., and Dobson, C.M. (1993) A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding. Biochemistry 32, 669-678
19. Nakano, T. and Fink, A.L. (1990) The folding of staphylococcal nuclease in the presence of methanol or guanidine thiocyanate. J. Biol. Chem. 265, 12356-12362
20. Fink, A.L. and Painter, B. (1987) Characterization of the unfolding of ribonuclease A in aqueous methanol solvents. Biochemistry 26, 1665-1671
21. Hiroto, N., Mizuno, K, and Goto, Y. (1997) Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol. Protein Sci. 6, 416-421
22. Kentsis, A. and Sosnick, T.R. (1998) Trifluoroethanol promotes helix formation by destabilizing backbone exposure: desolvation rather native hydrogen bonding defines the kinetic pathway of dimeric coiled coil folding. Biochemistry 37, 14613-14622
23. Luo, P. and Baldwin, R.L. (1997) Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry 36, 8413-8421
24. Jasanoff, A. and Fersht, A.R. (1994) Quantitative determination of helical propensities from trifluoroethanol titration curves. Biochemistry 33, 2129-2135
25. Hill, C.P., Osslund, T.D., and Eisenberg, D. (1993) The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors. Proc. Natl. Acad. Sci. USA 90, 5167-5171
26. Mott, H.R. and Campbell, I.D. (1995) Four-helix bundle growth factors and their receptors: protein-protein interactions. Curr. Opin. Struct. Biol. 5, 114-121
27. Manning, M.C., Patel, K., and Borchardt, R.T. (1989) Stability of protein pharmaceuticals. Pharm. Res. 6, 903-918
28. Smith, A.V. and Hall, C.K. (2001) Protein refolding versus aggregation: computer simulations on an intermediate-resolution protein model. J. Mol. Biol. 312, 187-202
29. Krishnan, S., Chi, E.Y., Webb, J.N., Chang, B.S., Shan, D., Goldenberg, M., Manning, M.C., Randolph, T.W., and Carpenter, J.F. (2002) Aggregation of granulocyte colony stimulating factor under physiological conditions: characterization and thermodynamic inhibition. Biochemistry 41, 6422-6431
30. Narhi, L.O., Kenney, W.C., and Arakawa, T. (1991) Conformational changes of recombinant human granulocyte-colony stimulating factor induced by pH and guanidine hydrochloride. J. Protein Chem. 10, 359-367
31. Kolvenbach, G.G., Elliott, S., Sachdev, R., Arakawa, T., and Narhi, L.O. (1993) Characterization of two fluorescent tryptophans in recombinant human granulocyte-colony stimulating factor: comparison of native sequence protein and tryptophan-deficient mutants. J. Protein Chem. 12, 229-236
32. Kolvenbach, C.G., Narhi, L.O., Philo, J.S., Li, T.S., Zhang, M., and Arakawa, T. (1997) Granulocyte-colony stimulating factor maintains a thermally stable, compact, partially folded structure at pH 2. J. Pept. Res. 50, 310-318
33. Yamazaki, K., Murayama, K., Ishikawa, R., and Ozaki, Y. (2005) An infrared spectroscopy study of acid stability and thermal unfolding process of granulocyte-colony stimulating factor. J. Biochem. 137, 265-271
34. Brems, D.N. (2002) The kinetics of G-CSF folding. Protein Sci. 11, 2504-2511
35. Pace, C.N. and Shaw, K.L. (2002) Linear extrapolation method of analyzing solvent denaturation curves. Proteins 4, 1-7
36. Pace, C.N. (1990) Measuring and increasing protein stability. Trends Biotechnol. 8, 93-98
37. Goto, Y., and Fink, A.L. (1989) Conformational states of β-lactamase: molten-globule states at acid and alkaline pH with high salt. Biochemistry 28, 945-952
38. Stryer, L. (1965) The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. J. Mol. Biol. 13, 482-495
39. Turner, D.C. and Brand, L. (1968) Quantitative estimation of protein binding site polarity. Biochemistry 7, 3381-3390
40. Fink, A.L. (1998) Protein aggregation: folding aggregates, inclusion bodies and amyloid. Folding Des. 3, R9-R23
41. Zink, T., Ross, A., Luers, K., Cieslar, C., Rudolph, R., and Holak, T.A. (1994) Structure and dynamics of the human granulocyte-colony stimulating factor determined NMR spectroscopy. Biochemistry 33, 8453-8463
42. Hirota, N., Mizuno, K., and Goto, Y. (1998) Group additive contributions to the alcohol-induced α-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins. J. Mol. Biol. 275, 365-378
43. Ptitsyn, O.B., Bychkova, V.E., and Uversky, V.N. (1995) Kinetic and equilibrium folding intermediates. Phil. Trans. R. Soc. Lond. B 348, 35-41
44. Yamazaki, K., Iwura, T., Ishikawa, R., and Ozaki, Y. Effect of ionic strength on the thermal unfolding process of granulocyte-colony stimulating factor. J. Biochem. in press.
45. Ogasawara, K., Matsushita, E., and Yutani, K. (1993) Further examination of the intermediate state in the denaturation of the tryptophan synthase a subunit. J. Mol. Biol. 234, 1197-1206
46. Yutani, K. and Ogasawara, K. (1992) Absence of the thermal transition in apo-α-lactalbumin in the molten globule state. J. Mol. Biol. 228, 347-350