In situ monitoring of proteins during lyophilization using micro-raman spectroscopy: A description of structural changes induced by dehydration

Journal of Pharmaceutical Sciences

Volumn 101, Issue 7, 2012, Pages 2316-2326

  Hédoux, Alain ^a   Paccou, Laurent ^a   Achir, Samira ^a   Guinet, Yannick ^a  

^a UNIVERSITÉ LILLE 1   (France)

Author keywords

Lyophilization; Protein structure; Proteins; Raman spectroscopy; Stability

Indexed keywords

AMIDE; BETA LACTOGLOBULIN; BOVINE SERUM ALBUMIN; CHYMOTRYPSINOGEN; SOLVENT; LACTOGLOBULIN; WATER;

ARTICLE; DENATURATION; DESORPTION; FREEZE DRYING; MONITORING; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; RAMAN SPECTROMETRY; ANIMAL; CATTLE; CHEMISTRY; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STABILITY;

ANIMALS; CATTLE; CHYMOTRYPSINOGEN; FREEZE DRYING; LACTOGLOBULINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STABILITY; SERUM ALBUMIN, BOVINE; SPECTRUM ANALYSIS, RAMAN; WATER;

EID: 84866290004     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23172     Document Type: Article

References (34)

1. Xiaolin T, Pikal MJ. 2005. The effects of stabilizers and denaturants on the cold denaturation temperatures of proteins and implications for freeze-drying. Pharm Res 22(7):1167-1175.
2. Wang W. 2000. Lyophilization and development of solid protein pharmaceuticals. Int J Pharm 203:1-60.
3. Franks F. 1998. Freeze-drying of bioproducts: Putting principles into practice. Eur J Pharm Biopharm 45:221-229.
4. Dill KA. 1990. Dominant forces in protein folding. Biochemistry 29:7133-7155.
5. Chang BS, Kendrick BS, Carpenter JF. 1996. Surface-induced denaturation of proteins during freezing and its inhibition by surfactants. J Pharm Sci 85(12):1325-1330.
6. Rupley JA, Careri G. 1991. Protein hydration and function. Adv Protein Chem 41:37-173.
7. Ngarize S, Herman H, Adams A, Howell N. 2004. Comparison of changes in the secondary structure of unheated, heated, and high-pressure-treated beta-lactoglobulin and ovalbumin proteins using Fourier transform Raman spectroscopy and self-deconvolution. J Agric Food Chem 52(21):6470-6477.
8. Freer ST, Kraut J, Robertus JD, Wright HT, Xuong NH. 1970. Chymotrypsinogen: 2.5-A crystal structure, comparison with α-chymotrypsin, and implication for zymogen activation. Biochemistry 9:1997-2009.
9. Anderle G, Mendelsohn R. 1987. Thermal denaturation of globular proteins. Fourier transform-infrared studies of the amide III spectral region. Biophys J 52(1):69-74.
10. Cai S, Singh BR. 1999. Identification of beta-turn and random coil amide III infrared bands for secondary structure estimation of proteins. Biophys Chem 80(1):7-20.
11. Seo J-A, Hedoux A, Guinet Y, Paccou L, Affouard F, Lerbret A, Descamps M. 2010. Thermal denaturation of beta-lactoglobulin and stabilization mechanism by trehalose analyzed from Raman spectroscopy investigations. J Phys Chem B 114:6675-6684.
12. Griko YV, Privalov PL. 1992. Calorimetric study of the heat and cold denaturation of beta-lactoglobulin. Biochemistry 31:8810-8815.
13. Panick G, Malessa R, Winter R. 1999. Differences between the pressure- and temperature-induced denaturation and aggregation of beta-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering. Biochemistry 38:6512-6519.
14. Hédoux A, Seo J-A, Guinet Y, Paccou L. 2011. Analysis of cold denaturation mechanism of β-lactoglobulin and comparison with thermal denaturation from Raman spectroscopy. J Raman Spectr. 43:16-23.
15. Hedoux A, Willart JF, Paccou L, Guinet Y, Affouard F, Lerbret A, Descamps M. 2009. Thermostabilization mechanism of bovine serum albumin by trehalose. J Phys Chem B 113(17):6119-6126.
16. Hawley SA. 1971. Reversible pressure-temperature denaturation of chymotrypsogen. Biochemistry 10:2436-2442.
17. Chalikian TG, Volker J, Anafi D, Breslauer KJ. 1997. The native and the heat-induced denatured states of α-chymotrysinogen A: Thermodynamic and spectroscopic studies. J Mol Biol 274:237-252.
18. Ionov R, Hédoux A, Guinet Y, Bordat P, Lerbret A, Affouard F, Prevost D, Descamps M. 2006. Sugar bioprotective effects on thermal denaturation of lysozyme: Insights from Raman scattering experiments and molecular dynamics simulation. J Non-Crystalline Solids 352:4430-4436.
19. Hédoux A, Ionov R, Willart JF, Lerbret A, Affouard F, Guinet Y, Descamps M, Prevost D, Paccou L, Danède F. 2006. Evidence of a two-stage thermal denaturation process in lysozyme: A Raman scattering and differential scanning calorimetry investigation. J Chem Phys 124:14703-14709.
20. Hédoux A, Krenzlin S, Paccou L, Guinet Y, Flament M-P, Siepmann J. 2010. Influence of urea and guanidine hydrochloride on lysozyme stability and thermal denaturation: A correlation between activity, protein dynamics and conformational changes. Phys Chem Chem Phys 12(40):13189-13196.
21. Hédoux A, Guinet Y, Paccou L. 2011. Analysis of the mechanism of lysozyme pressure denaturation from Raman spectroscopy investigations, and comparison with thermal denaturation. J Phys Chem B 115:6740-6748.
22. Remmele RL Jr., Stushnoff C, Carpenter JF. 1997. Real-time in situ monitoring of lysozyme during lyophilization using infrared spectroscopy: Dehydration stress in the presence of sucrose. Pharm Res 14(11):1548-1555.
23. Remmele RL Jr., Stushnoff C. 1994. Low-temperature IR spectroscopy reveals four stages of water loss during lyophilization of hen egg white lysozyme. Biopolymers 34:365-370.
24. Williams RW, Dunker AK. 1981. Determination of the secondary structure of proteins from the amide I band of the laser Raman spectrum. J Mol Biol 152(4):783-813.
25. Surewicz WK, Mantsch HH, Chapman D. 1993. Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment. Biochemistry 32(2):389-394.
26. Murphy WF, Bernstein HJ. 1972. Raman spectra and assignment of the vibrational stretching region of water. J Phys Chem 76(8):1147-1152.
27. Scherer JR, Go MK, Kint S. 1974. Raman spectra and structure of water from -10 to 90°. J Phys Chem 78(13):1304-1313.
28. Allison S, Chang B, Randolph T, Carpenter JF. 1999. Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding. Arch Biochem Biophys 365(2):289-298.
29. Allison SD, Dong A, Carpenter JF. 1996. Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying, and rehydration. Biophys J 71:2022-2032.
30. Prestrelski SJ, Arakawa T, Carpenter JF. 1993. Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization. II. Structural studies using infrared spectroscopy. Arch Biochem Biophys 303(2):465-473.
31. Prestrelski SJ, Tedeschi N, Arakawa T, Carpenter JF. 1993. Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophys J 65(2):661-671.
32. Prestrelski SJ, Pikal KA, Arakawa T. 1995. Optimization of lyophilization conditions for recombinant human interleukin-2 by dried-state conformational analysis using Fourier-transform infrared spectroscopy. Pharm Res 12(9):1250-1259.
33. Kendrick BS, Dong A, Allison SD, Manning MC, Carpenter JF. 1996. Quantitation of the area overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states. J Pharm Sci 85(2):155-158.
34. Willart JF, De Gusseme A, Hemon S, Descamps M, Leveiller F, Rameau A. 2002. Vitrification and polymorphism of trehalose induced by dehydration of trehalose dihydrate. J Phys Chem B 106(13):501-505.