Structure-based analysis reveals hydration changes induced by arginine hydrochloride

Biophysical Chemistry

Volumn 137, Issue 2-3, 2008, Pages 105-109

  Nakakido, Makoto ^a   Tanaka, Yoshikazu ^a,b   Mitsuhori, Mariko ^a   Kudou, Motonori ^a   Ejima, Daisuke ^c   Arakawa, Tsutomu ^d   Tsumoto, Kouhei ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b HOKKAIDO UNIVERSITY   (Japan)

^c AJINOMOTO CO INC   (Japan)

^d ALLIANCE PROTEIN LABORATORIES   (United States)

Author keywords

Arginine hydrochloride; Crystal structure; Hydration water molecules; Lysozyme; Protein aggregation; Refolding

Indexed keywords

ARGININE; LYSOZYME;

ARTICLE; CONTROLLED STUDY; ENZYME BINDING; ENZYME STRUCTURE; HYDRATION; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

ANIMALS; ARGININE; BETAINE; CHICKENS; CRYSTALLOGRAPHY, X-RAY; EGG PROTEINS; MODELS, MOLECULAR; MURAMIDASE; PROTEIN STRUCTURE, TERTIARY; SODIUM CHLORIDE; SUCROSE; WATER;

EID: 51649101489     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2008.07.009     Document Type: Article

References (45)

1. Tsumoto K., Ejima D., Kumagai I., and Arakawa T. Practical considerations in refolding proteins from inclusion bodies. Protein Expr. Purif. 28 (2003) 1-8
2. Clark E.D. Protein refolding for industrial processes. Curr. Opin. Biotechnol. 12 (2001) 202-207
3. Yasuda M., Murakami Y., Sowa A., Ogino H., and Ishikawa H. Effect of additives on refolding of a denatured protein. Biotechnol. Prog. 14 (1998) 601-606
4. Hamada H., and Shiraki K. l-argininamide improves the refolding more effectively than l-arginine. J. Biotechnol. 130 (2007) 153-160
5. Shiraki K., Kudou M., Fujiwara S., Imanaka T., and Takagi M. Biophysical effect of amino acids on the prevention of protein aggregation. J. Biochem. 132 (2002) 591-595
6. Yamaguchi S., Yamamoto E., Tsukiji S., and Nagamune T. Successful control of aggregation and folding rates during refolding of denatured lysozyme by adding N-methylimidazolium cations with various N'-substituents. Biotechnol. Prog. 24 (2008) 402-408
7. Cash H.L., Whitham C.V., and Hooper L.V. Refolding, purification, and characterization of human and murine RegIII proteins expressed in Escherichia coli. Protein Expr. Purif. 48 (2006) 151-159
8. Takahashi S., Ogasawara H., Watanabe T., Kumagai M., Inoue H., and Hori K. Refolding and activation of human prorenin expressed in Escherichia coli: application of recombinant human renin for inhibitor screening. Biosci. Biotechnol. Biochem. 70 (2006) 2913-2918
9. Bajorunaite E., Sereikaite J., and Bumelis V.A. l-arginine suppresses aggregation of recombinant growth hormones in refolding process from E. coli inclusion bodies. Protein. J. 26 (2007) 547-555
10. Tsumoto K., Shinoki K., Kondo H., Uchikawa M., Juji T., and Kumagai I. Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent-application to a human single-chain Fv fragment. J. Immunol. Methods 219 (1998) 119-129
11. Wan L., Zeng L., Chen L., Huang Q., Li S., Lu Y., Li Y., Cheng J., and Lu X. Expression, purification, and refolding of a novel immunotoxin containing humanized single-chain fragment variable antibody against CTLA4 and the N-terminal fragment of human perforin. Protein Expr. Purif. 48 (2006) 307-313
12. Clement G., Boquet D., Mondoulet L., Lamourette P., Bernard H., and Wal J.M. Expression in Escherichia coli and disulfide bridge mapping of PSC33, an allergenic 2S albumin from peanut. Protein Expr. Purif. 44 (2005) 110-120
13. Arakawa T., Tsumoto K., Kita Y., Chang B., and Ejima D. Biotechnology applications of amino acids in protein purification and formulations. Amino Acids 33 (2007) 587-605
14. Tsumoto K., Umetsu M., Kumagai I., Ejima D., Philo J.S., and Arakawa T. Role of arginine in protein refolding, solubilization, and purification. Biotechnol. Prog. 20 (2004) 1301-1308
15. Reddy K.R., Lilie H., Rudolph R., and Lange C. l-Arginine increases the solubility of unfolded species of hen egg white lysozyme. Protein Sci. 14 (2005) 929-935
16. Arakawa T., and Tsumoto K. The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation. Biochem. Biophys. Res. Commun. 304 (2003) 148-152
17. Umetsu M., Tsumoto K., Nitta S., Adschiri T., Ejima D., Arakawa T., and Kumagai I. Nondenaturing solubilization of beta2 microglobulin from inclusion bodies by l-arginine. Biochem. Biophys. Res. Commun. 328 (2005) 189-197
18. Tsumoto K., Umetsu M., Kumagai I., Ejima D., and Arakawa T. Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine. Biochem. Biophys. Res. Commun. 312 (2003) 1383-1386
19. Ejima D., Yumioka R., Tsumoto K., and Arakawa T. Effective elution of antibodies by arginine and arginine derivatives in affinity column chromatography. Anal. Biochem. 345 (2005) 250-257
20. Arakawa T., Philo J.S., Tsumoto K., Yumioka R., and Ejima D. Elution of antibodies from a Protein-A column by aqueous arginine solutions. Protein Expr. Purif. 36 (2004) 244-248
21. Tsumoto K., Ejima D., Nagase K., and Arakawa T. Arginine improves protein elution in hydrophobic interaction chromatography. The cases of human interleukin-6 and activin-A. J. Chromatogr. A 1154 (2007) 81-86
22. Tsumoto K., Ejima D., Senczuk A.M., Kita Y., and Arakawa T. Effects of salts on protein-surface interactions: applications for column chromatography. J. Pharm. Sci. 96 (2007) 1677-1690
23. Arakawa T., Ejima D., Tsumoto K., Ishibashi M., and Tokunaga M. Improved performance of column chromatography by arginine: dye-affinity chromatography. Protein Expr. Purif. 52 (2007) 410-414
24. Ejima D., Yumioka R., Arakawa T., and Tsumoto K. Arginine as an effective additive in gel permeation chromatography. J. Chromatogr. A 1094 (2005) 49-55
25. Tobias D.J., and Hemminger J.C. Chemistry. Getting specific about specific ion effects. Science 319 (2008) 1197-1198
26. Nakasako M. Water-protein interactions from high-resolution protein crystallography. Philos. Trans. R. Soc. Lond., B Biol. Sci. 359 (2004) 1191-1204 [discussion 1204-6]
27. Mattos C., Bellamacina C.R., Peisach E., Pereira A., Vitkup D., Petsko G.A., and Ringe D. Multiple solvent crystal structures: probing binding sites, plasticity and hydration. J. Mol. Biol. 357 (2006) 1471-1482
28. Jiang J.S., and Brunger A.T. Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243 (1994) 100-115
29. Higo J., and Nakasako M. Hydration structure of human lysozyme investigated by molecular dynamics simulation and cryogenic X-ray crystal structure analyses: on the correlation between crystal water sites, solvent density, and solvent dipole. J. Comput. Chem. 23 (2002) 1323-1336
30. Schlessman J.L., Abe C., Gittis A., Karp D.A., Dolan M.A., and Garcia-Moreno E.B. Crystallographic study of hydration of an internal cavity in engineered proteins with buried polar or ionizable groups. Biophys. J. 94 (2008) 3208-3216
31. Rayment I. Small-scale batch crystallization of proteins revisited: an underutilized way to grow large protein crystals. Structure 10 (2002) 147-151
32. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Macromol. Crystallogr. Pt A 276 (1997) 307-326
33. McRee D.E. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
34. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr., D Biol. Crystallogr. 53 (1997) 240-255
35. Laskowski R.A., Macarthur M.W., Moss D.S., and Thornton J.M. Procheck - a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26 (1993) 283-291
36. Lee J.C., and Timasheff S.N. The stabilization of proteins by sucrose. J. Biol. Chem. 256 (1981) 7193-7201
37. Arakawa T., and Timasheff S.N. Preferential interactions of proteins with solvent components in aqueous amino acid solutions. Arch. Biochem. Biophys. 224 (1983) 169-177
38. Felitsky D.J., Cannon J.G., Capp M.W., Hong J., Van Wynsberghe A.W., Anderson C.F., and Record Jr. M.T. The exclusion of glycine betaine from anionic biopolymer surface: why glycine betaine is an effective osmoprotectant but also a compatible solute. Biochemistry 43 (2004) 14732-14743
39. Arakawa T., Ejima D., Tsumoto K., Obeyama N., Tanaka Y., Kita Y., and Timasheff S.N. Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects. Biophys. Chem. 127 (2007) 1-8
40. Ishibashi M., Tsumoto K., Tokunaga M., Ejima D., Kita Y., and Arakawa T. Is arginine a protein-denaturant?. Protein Expr. Purif. 42 (2005) 1-6
41. Lyutova E.M., Kasakov A.S., and Gurvits B.Y. Effects of arginine on kinetics of protein aggregation studied by dynamic laser light scattering and tubidimetry techniques. Biotechnol. Prog. 23 (2007) 1411-1416
42. Arakawa T., and Timasheff S.N. Preferential interactions of proteins with salts in concentrated solutions. Biochemistry 21 (1982) 6545-6552
43. Kita Y., Arakawa T., Lin T.Y., and Timasheff S.N. Contribution of the surface free energy perturbation to protein-solvent interactions. Biochemistry 33 (1994) 15178-15189
44. Lin T.Y., and Timasheff S.N. On the role of surface tension in the stabilization of globular proteins. Protein Sci. 5 (1996) 372-381
45. Mande S.C., and Sobhia M.E. Structural characterization of protein-denaturant interactions: crystal structures of hen egg-white lysozyme in complex with DMSO and guanidinium chloride. Protein Eng. 13 (2000) 133-141