Infrared microscopy for in situ measurement of protein secondary structure during freezing and freeze-drying

Journal of Pharmaceutical Sciences

Volumn 96, Issue 1, 2007, Pages 179-195

  Schwegman, J Jeff ^a,b   Carpenter, John F ^c   Nail, Steven L ^a,d  

^a PURDUE UNIVERSITY   (United States)

^b BioConvergence LLC   (United States)

^c UNIVERSITY OF COLORADO   (United States)

^d Baxter Pharmaceutical Solutions LLC   (United States)

Author keywords

Biotechnology; Drying; Infrared spectroscopy; Injectables; Lyophilization; Protein formulation

Indexed keywords

BETA LACTOGLOBULIN; CATALASE; LACTATE DEHYDROGENASE; MANNITOL; SUCROSE;

ARTICLE; FREEZE DRYING; FREEZING; INFRARED RADIATION; INFRARED SPECTROSCOPY; INTERMETHOD COMPARISON; MICROSCOPY; PHASE TRANSITION; PROTEIN ANALYSIS; PROTEIN SECONDARY STRUCTURE; SENSITIVITY ANALYSIS; SIGNAL NOISE RATIO; SPECTROMETRY; WATER VAPOR;

EID: 33846131221     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.20630     Document Type: Article

References (28)

1. Byler DM, Susi H. 1986. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25:469-487.
2. Carpenter JF, Crowe JH. 1989. An infrared spectroscopic study of the interactions of carbohydrates with dried proteins. Biochemistry 28:3916-3922.
3. Carpenter JF, Prestrelski SJ, Dong A. 1998. Application of infrared spectroscopy to development of stable lyophilized protein formulations. Eur J Pharm Biopharm 45:231-238.
4. Dong A, Huang P, Caughey WS. 1990. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29:3303-3308.
5. Jackson M, Mantsch HH. 1995. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit Rev Biochem Mol Biol 30:95-120.
6. Surewicz WK, Mantsch HH. 1988. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim Biophys Acta 952:115-130.
7. Susi H, Byler DM. 1983. Protein structure by Fourier transform infrared spectroscopy: Second derivative spectra. Biochem Biophys Res Commun 115:391-397.
8. Chan HK, Ongpipattanakul B, Au-Yeung J. 1996. Aggregation of rhDNase occurred during the compression of KBr pellets used for FTIR spectroscopy. Pharm Res 13:238-242.
9. Souillac PO, Middaugh CR, Rytting JH. 2002. Investigation of protein/carbohydrate interactions in the dried state. 2. Diffuse reflectance FTIR studies. Int J Pharm 235:207-218.
10. Casal HL, Kohler U, Mantsch HH. 1988. Structural and conformational changes of beta-lactoglobulin B: An infrared spectroscopic study of the effect of pH and temperature. Biochim Biophys Acta 957:11-20.
11. Hillgren A, Lindgren J, Alden M. 2002. Protection mechanism of Tween 80 during freeze-thawing of a model protein, LDH. Int J Pharm 237:57-69.
12. 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 14:1548-1555.
13. Dong A, Matsuura J, Allison SD, Chrisman E, Manning MC, Carpenter JF. 1996. Infrared and circular dichroism spectroscopic characterization of structural differences between beta-lactoglobulin A and B. Biochemistry 35:1450-1457.
14. Dong AC, Huang P, Caughey WS. 1992. Redox-dependent changes in beta-extended chain and turn structures of cytochrome c in water solution determined by second derivative amide I infrared spectra. Biochemistry 31:182-189.
15. Prestrelski SJ, Byler DM, Liebman MN. 1991. Comparison of various molecular forms of bovine trypsin: Correlation of infrared spectra with X-ray crystal structures. Biochemistry 30:133-143.
16. Susi H, Byler DM. 1986. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol 130:290-311.
17. Kendrick BS, Dong A, Allison SD, Manning MC, Carpenter JF. 1996. Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states. J Pharm Sci 85:155-158.
18. Dong A, Prestrelski SJ, Allison SD, Carpenter JF. 1995. Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. J Pharm Sci 84:415-424.
19. Clark AH, Tuffnell CD. 1980. Small-angle x-ray scattering studies of thermally-induced globular protein gels. Int J Pept Protein Res 16:339-351.
20. Chang BS, Kendrick BS, Carpenter JF. 1996. Surface-induced denaturation of proteins during freezing and its inhibition by surfactants. J Pharm Sci 85:1325-1330.
21. Anchordoquy TJ, Carpenter JF. 1996. Polymers protect lactate dehydrogenase during freeze-drying by inhibiting dissociation in the frozen state. Arch Biochem Biophys 332:231-238.
22. Arakawa T, Prestrelski SJ, Kenney WC, Carpenter JF. 2001. Factors affecting short-term and long-term stabilities of proteins. Adv Drug Deliv Rev 46:307-326.
23. Carpenter JF, Pikal MJ, Chang BS, Randolph TW. 1997. Rational design of stable lyophilized protein formulations: Some practical advice. Pharm Res 14:969-975.
24. Sarciaux JM, Mansour S, Hageman MJ, Nail SL. 1999. Effects of buffer composition and processing conditions on aggregation of bovine IgG during freeze-drying. J Pharm Sci 88:1354-1361.
25. Griebenow K, Klibanov AM. 1995. Lyophilization-induced reversible changes in the secondary structure of proteins. Proc Natl Acad Sci USA 92:10969-10976.
26. Prestrelski SJ, Tedeschi N, Arakawa T, Carpenter JF. 1993. Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophys J 65:661-671.
27. Carpenter JF, Chang B, Randolph TW. 2004. Physical damage to proteins during freezing, drying, and rehydration. In: Constantino HR, Pikal MJ, editors. Lyophilization of biopharmaceuticals, edn. Arlington, VA: American Association of Pharmaceutical Scientists, pp 423-443.
28. Chirgadze YN, Fedorov OV, Trushina NP. 1975. Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water. Biopolymers 14:679-694.