Conformational and bioactivity analysis of insulin: Freeze-drying TBA/water co-solvent system in the presence of surfactant and sugar

International Journal of Pharmaceutics

Volumn 371, Issue 1-2, 2009, Pages 71-81

  Yong, Zhang ^a   Yingjie, Deng ^a   Xueli, Wang ^b   Jinghua, Xu ^a   Zhengqiang, Li ^b  

^a SHENYANG PHARMACEUTICAL UNIVERSITY   (China)

^b JILIN UNIVERSITY   (China)

Author keywords

Alcohol; Bioactivity; Co solvent; Conformation; Insulin; Lyophilization; Sugar; Surfactant

Indexed keywords

BILE SALT; INSULIN; SOLVENT; SUGAR; SURFACTANT; TERT BUTYL ALCOHOL; TREHALOSE; WATER;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DIABETES MELLITUS; DRUG ACTIVITY; DRUG CONFORMATION; DRUG FORMULATION; FLUORESCENCE SPECTROSCOPY; FREEZE DRYING; INFRARED SPECTROSCOPY; MALE; MOUSE; NONHUMAN; PRIORITY JOURNAL; SOLID STATE; ULTRAVIOLET SPECTROSCOPY;

ANIMALS; BILE ACIDS AND SALTS; DIABETES MELLITUS, EXPERIMENTAL; DRUG COMPOUNDING; DRUG STABILITY; DRUG STORAGE; FREEZE DRYING; HYPOGLYCEMIC AGENTS; INSULIN; MALE; MICE; MICE, INBRED STRAINS; PROTEIN CONFORMATION; PROTEIN STABILITY; SOLVENTS; SURFACE-ACTIVE AGENTS; TERT-BUTYL ALCOHOL; TREHALOSE; WATER;

EID: 62849122418     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2008.12.018     Document Type: Article

References (59)

1. Allison S.D., Chang B., Randolph T.W., and Carpenter J.F. Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding. Arch. Biochem. Biophys. 365 (1999) 289-298
2. Allison S.D., Randolph T.W., Manning M.C., Middleton K., Davis A., and Carpenter J.F. Effects of drying methods and additives on structure and function of act mechanisms of dehydration-induced damage its inhibition. Arch. Biochem. Biophys. 358 (1998) 171-181
3. Arunkumar A.I., Kumar T.K., and Yu C. Non-specific helix-induction in charged homopolypeptides by alcohols. Biochim. Biophys. Acta 1338 (1997) 69-76
4. Brandts J.F., and Kaplan L.J. Derivative sspectroscopy applied to tyrosyl chromophores. Studies on ribonuclease, lima bean inhibitors, insulin, and pancreatic trypsin inhibitor. Biochemistry 12 (1973) 2011-2024
5. Byler D.M., and Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25 (1986) 469-487
6. Carpenter J.F., and Crowe J.H. The mechanism of cryoprotection of proteins by solutes. Cryobiology 25 (1988) 244-255
7. Chang B.S., Beauvais R.M., Dong A., and Carpenter J.F. Physical factors affecting the storage stability of freeze-dried interleukin-1 receptor antagonist: glass transition and protein conformation. Arch. Biochem. Biophys. 331 (1996) 249-258
8. Chang L.L., Shepherd D., Sun J., Ouellette D., Grant K.L., Tang X.C., and Pikal M.J. Mechanism of protein stabilization by sugars during freeze-drying and storage: native structure preservation, specific interaction, and/or immobilization in a glassy matrix?. J. Pharm. Sci. 94 (2005) 1427-1444
9. Costantino H.R., Carrasquillo K.G., Cordero R.A., Mumenthaler M., Hsu C.C., and Griebenow K. Effect of excipients on the stability and structure of lyophilized recombinant human growth hormone. J. Pharm. Sci. 87 (1998) 1412-1420
10. Costantino H.R., Griebenow K., Mishra P., Langer R., and Klibanov A.M. Fourier-transform infrared spectroscopic investigation of protein stability in the lyophilized form. Biochim. Biophys. Acta 1253 (1995) 69-74
11. Demelier J.F., Labat J., and Courtois J.E. Influence of parenterally injected trehalose in mammals having trehalase activity at different sites. Ann. Biol. Clin. 33 (1975) 297-302
12. Dixit S., Crain J., Poon W.C., Finney J.L., and Soper A.K. Molecular segregation observed in a concentrated alcohol-water solution. Nature 416 (2002) 829-832
13. Dong A., Huang P., and Caughey W.S. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29 (1990) 3303-3308
14. Dong A., Meyer J.D., Kendrick B.S., Manning M.C., and Carpenter J.F. Effect of secondary structure on the activity of enzymes suspended in organic solvents. Arch. Biochem. Biophys. 334 (1996) 406-414
15. Fioroni M., Diaz M.D., Burger K., and Berger S. Solvation phenomena of a tetrapeptide in water/trifluoroethanol and water/ethanol mixtures: a diffusion NMR, intermolecular NOE, and molecular dynamics study. J. Am. Chem. Soc. 124 (2002) 7737-7744
16. Griebenow K., and Klibanov A.M. Lyophilization-induced reversible changes in the secondary structure of proteins. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 10969-10976
17. Han B., Hall F.L., and Nimni M.E. Refolding of a recombinant collagen-targeted TGF-beta2 fusion protein expressed in Escherichia coli. Protein Expr. Purif. 11 (1997) 169-178
18. Head-Gordon T. Is water structure around hydrophobic groups clathrate-like?. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 8308-8312
19. Heller M.C., Carpenter J.F., and Randolph T.W. Protein formulation and lyophilization cycle design: prevention of damage due to freeze-concentration induced phase separation. Biotechnol. Bioeng. 63 (1999) 166-174
20. Hirota N., Mizuno K., and Goto Y. Group additive contributions to the alcohol-induced alpha-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins. J. Mol. Biol. 275 (1998) 365-378
21. Jayaraman G., Kumar T.K., Arunkumar A.I., and Yu C. 2,2,2-Trifluoroethanol induces helical conformation in an all beta-sheet protein. Biochem. Biophys. Res. Commun. 222 (1996) 33-37
22. Kasraian K., and DeLuca P.P. The effect of tertiary butyl alcohol on the resistance of the dry product layer during primary drying. Pharm. Res. 12 (1995) 491-495
23. Kasraian K., and DeLuca P.P. Thermal analysis of the tertiary butyl alcohol-water system and its implications on freeze-drying. Pharm. Res. 12 (1995) 484-490
24. Kaushik J.K., and Bhat R. Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose. J. Biol. Chem. 278 (2003) 26458-26465
25. Kim Y., and Shields J.E. pH dependent conformational changes in the T- and R-states of insulin in solution: circular dichroic studies in the pH range of 6 to 10. Biochem. Biophys. Res. Commun. 186 (1992) 1115-1120
26. Li C.L., and Deng Y.J. Oil-based formulations for oral delivery of insulin. J. Pharm. Pharmacol. 56 (2004) 1101-1107
27. Liao Y.H., Brown M.B., and Martin G.P. Investigation of the stabilisation of freeze-dried lysozyme and the physical properties of the formulations. Eur. J. Pharm. Biopharm. 58 (2004) 15-24
28. Liu J. Physical characterization of pharmaceutical formulations in frozen and freeze-dried solid states: techniques and applications in freeze-drying development. Pharm. Dev. Technol. 11 (2006) 3-28
29. Luthra S., Obert J.P., Kalonia D.S., and Pikal M.J. Impact of critical process and formulation parameters affecting in-process stability of lactate dehydrogenase during the secondary drying stage of lyophilization: a mini freeze dryer study. J. Pharm. Sci. 96 (2007) 2242-2250
30. Melberg G.S., and Johnson W.C.J. Changes in secondary structure follow the dissociation of human insulin hexamers: a circular dichroism study. Proteins Struct. Funct. Genet. 8 (1990) 280-286
31. Menendez C.J., and Herskovits T.T. Studies of the location of the tyrosyl residues in insulin II. Biochemistry 8 (1969) 5052-5059
32. Menendez C.J., Herskovits T.T., and Laskowski Jr. M. Studies of the location of the tyrosyl residues in insulin I. Biochemistry 8 (1969) 5044-5051
33. Morita T., Horikiri Y., Yamahara H., Suzuki T., and Yoshino H. Formation and isolation of spherical fine protein microparticles through lyophilization of protein-poly(ethylene glycol) aqueous mixture. Pharm. Res. 17 (2000) 1367-1373
34. Oberg K.A., and Fink A.L. A new attenuated total reflectance Fourier transform infrared spectroscopy method for the study of proteins in solution. Anal. Biochem. 256 (1998) 92-106
35. Oh K.S., Han S.K., Lee H.S., Koo H.M., Kim R.S., Lee K.E., Han S.S., Cho S.H., and Yuk S.H. Core/shell nanoparticles with lecithin lipid cores for protein delivery. Biomacromolecules 7 (2006) 2362-2367
36. Paris N., Rentier-Delrue F., Defontaine A., Goffin V., Lebrun J.J., Mercier L., and Martial J.A. Bacterial production and purification of recombinant human prolactin. Biotechnol. Appl. Biochem. 12 (1990) 436-449
37. Passot S., Fonseca F., Alarcon-Lorca M., Rolland D., and Marin M. Physical characterisation of formulations for the development of two stable freeze-dried proteins during both dried and liquid storage. Eur. J. Pharm. Biopharm. 60 (2005) 335-348
38. Pocker Y., and Biswas S.B. Conformational dynamics of insulin in solution circular dichroic studies. Biochemistry 19 (1980) 5043-5049
39. Prestrelski S.J., Tedeschi N., Arakawa T., and Carpenter J.F. Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophys. J. 65 (1993) 661-671
40. Rey L. Potential prospects in freeze-drying. In: Rey L., and May J.C. (Eds). Freeze-Drying/Lyophilization of Pharmaceuticals and Biological Products (1999), Marcel Dekker, New York 470-471
41. Rock C.O. Environment of the aromatic chromophores of acyl carrier protein. Arch. Biochem. Biophys. 225 (1983) 122-129
42. Sarmento B., Ferreira D.C., Jorgensen L., and van de Weert M. Probing insulin's secondary structure after entrapment into alginate/chitosan nanoparticles. Eur. J. Pharm. Biopharm. 65 (2007) 10-17
43. Sinibaldi R., Casieri C., Melchionna S., Onori G., Segre A.L., Viel S., Mannina L., and De Luca F. The role of water coordination in binary mixtures. A study of two model amphiphilic molecules in aqueous solutions by molecular dynamics and NMR. J. Phys. Chem. B 110 (2006) 8885-8892
44. Small D.M. The bile acids. In: Nair P.P., and Kritchevsky D. (Eds). Physiology and Metabolism (1971), Plenum Press, New York 302-326
45. Sen S., Dutta P., Mukherjee S., and Bhattacharyya K. Solvation dynamics in bile salt aggregates. J. Phys. Chem. B 106 (2002) 7745-7750
46. Souillac P.O., Middaugh C.R., and Rytting J.H. Investigation of protein/carbohydrate interactions in the dried state 2. Diffuse reflectance FTIR studies. Int. J. Pharm. 235 (2002) 207-218
47. Teagarden D.L., and Baker D.S. Practical aspects of lyophilization using non-aqueous co-solvent systems. Eur. J. Pharm. Sci. 15 (2002) 115-133
48. 1, U.S. Patent 5,770,230.
49. Telang C., and Suryanarayanan R. Crystallization of cephalothin sodium during lyophilization from tert-butyl alcohol-water cosolvent system. Pharm. Res. 22 (2005) 153-160
50. Thomas P.D., and Dill K.A. Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation. Protein Sci. 2 (1993) 2050-2065
51. Tran-Moseman A., Schauer N., and De Bernardez Clark E. Renaturation of Escherichia coli-derived recombinant human macrophage colony-stimulating factor. Protein Expr. Purif. 16 (1999) 181-189
52. Unneberg P., Merelo J.J., Chacon P., and Moran F. SOMCD: method for evaluating protein secondary structure from UV circular dichroism spectra. Proteins 42 (2001) 460-470
53. Van Drooge D.J., Hinrichs W.L., and Frijlink H.W. Incorporation of lipophilic drugs in sugar glasses by lyophilization using a mixture of water and tertiary butyl alcohol as solvent. J. Pharm. Sci. 93 (2004) 713-725
54. Vecchio G., Bossi A., Pasta P., and Carrea G. Fourier-transform infrared conformational study of bovine insulin in surfactant solutions. Int. J. Pept. Protein Res. 48 (1996) 113-117
55. Wang W. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int. J. Pharm. 185 (1999) 129-188
56. Wang W. Lyophilization and development of solid protein pharmaceuticals. Int. J. Pharm. 203 (2000) 1-60
57. Wei J.A., Lin Y.Z., Zhou J.M., and Tsou C.L. FTIR studies of secondary structures of bovine insulin and its derivatives. Biochim. Biophys. Acta 1080 (1991) 29-33
58. Wittaya-Areekul S., Needham G.F., Milton N., Roy M.L., and Nail S.L. Freeze-drying of tert-butanol/water cosolvent systems: a case report on formation of a friable freeze-dried powder of tobramycin sulfate. J. Pharm. Sci. 91 (2002) 1147-1155
59. Zana R., and Eljebari M.J. Fluorescence probing investigation of the self-association of alcohols in aqueous solution. J. Phys. Chem. 97 (1993) 11134-11136