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Volumn 45, Issue 3, 1998, Pages 231-238

Application of infrared spectroscopy to development of stable lyophilized protein formulations

Author keywords

Infrared spectroscopy; Lyophilization; Protein formulation

Indexed keywords

DRUG FORMULATION; FREEZE DRYING; INFRARED SPECTROSCOPY; PROTEIN DENATURATION; PROTEIN MODIFICATION; PROTEIN PROCESSING; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW; STORAGE;

EID: 0032078387     PISSN: 09396411     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0939-6411(98)00005-8     Document Type: Review
Times cited : (144)

References (22)
  • 2
    • 0027163348 scopus 로고
    • Dehydration-induced conformational changes in proteins and their inhibition by stabilizers
    • [2] S.J. Prestrelski, N. Tedeschi, T. Arakawa, J.F. Carpenter, Dehydration-induced conformational changes in proteins and their inhibition by stabilizers, Biophys. J. 65 (1993) 661-671.
    • (1993) Biophys. J. , vol.65 , pp. 661-671
    • Prestrelski, S.J.1    Tedeschi, N.2    Arakawa, T.3    Carpenter, J.F.4
  • 3
    • 0027176042 scopus 로고
    • Separation of freezing-and drying-induced denaturation of lyophilized proteins by stress-specific stabilization: : II. Structural studies using infrared spectroscopy
    • [3] S.J. Prestrelski, T. Arakawa, J.F. Carpenter, Separation of freezing-and drying-induced denaturation of lyophilized proteins by stress-specific stabilization: : II. Structural studies using infrared spectroscopy, Arch. Biochem. Biophys. 303 (1993) 465-473.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 465-473
    • Prestrelski, S.J.1    Arakawa, T.2    Carpenter, J.F.3
  • 4
    • 0001159547 scopus 로고
    • The structure of proteins in lyophilized formulations using Fourier transform infrared spectroscopy. Formulation and delivery of proteins and peptides
    • [4] S.J. Prestrelski, T. Arakawa, J.F. Carpenter, The structure of proteins in lyophilized formulations using Fourier transform infrared spectroscopy. Formulation and delivery of proteins and peptides, Am. Chem. Soc. Symp. Series 567 (1994) 148-169.
    • (1994) Am. Chem. Soc. Symp. Series , vol.567 , pp. 148-169
    • Prestrelski, S.J.1    Arakawa, T.2    Carpenter, J.F.3
  • 5
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization-and temperature-induced protein aggregation
    • [5] A. Dong, S.J. Prestrelski, S.D. Allison, J.F. Carpenter, Infrared spectroscopic studies of lyophilization-and temperature-induced protein aggregation, J. Pharm. Sci. 84 (1995) 415-424.
    • (1995) J. Pharm. Sci. , vol.84 , pp. 415-424
    • Dong, A.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 6
    • 0028865701 scopus 로고
    • Optimization of lyophilization conditions for recombinant human interleukin-2 by dried-state conformational analysis using Fourier transform infrared spectroscopy
    • [6] S.J. Prestrelski, K.A. Pikal, T. Arakawa, Optimization of lyophilization conditions for recombinant human interleukin-2 by dried-state conformational analysis using Fourier transform infrared spectroscopy, Pharm. Res. 12 (1995) 1250-1259.
    • (1995) Pharm. Res. , vol.12 , pp. 1250-1259
    • Prestrelski, S.J.1    Pikal, K.A.2    Arakawa, T.3
  • 7
    • 0030586287 scopus 로고    scopus 로고
    • Physical factors affecting the storage stability of freeze-dried interleukin-1 receptor antagonist: Glass transition and protein conformation
    • [7] B.S. Chang, R.M. Beauvais, A. Dong, J.F. Carpenter, 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.
    • (1996) Arch. Biochem. Biophys. , vol.331 , pp. 249-258
    • Chang, B.S.1    Beauvais, R.M.2    Dong, A.3    Carpenter, J.F.4
  • 8
    • 0029815193 scopus 로고    scopus 로고
    • Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying and rehydration
    • [8] S.D. Allison, A. Dong, J.F. Carpenter, Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying and rehydration, Biophys. J. 71 (1996) 2022-2032.
    • (1996) Biophys. J. , vol.71 , pp. 2022-2032
    • Allison, S.D.1    Dong, A.2    Carpenter, J.F.3
  • 9
    • 0025877453 scopus 로고
    • Protein hydration and function
    • [9] J.A. Rupley, G. Careri, Protein hydration and function, Adv. Protein Chem. 41 (1991) 37-172.
    • (1991) Adv. Protein Chem. , vol.41 , pp. 37-172
    • Rupley, J.A.1    Careri, G.2
  • 10
    • 0016022523 scopus 로고
    • Hydration of proteins and polypeptides
    • [10] I.D. Kuntz, W. Kauzman, Hydration of proteins and polypeptides, Adv. Protein Chem. 28 (1974) 239-345.
    • (1974) Adv. Protein Chem. , vol.28 , pp. 239-345
    • Kuntz, I.D.1    Kauzman, W.2
  • 11
    • 0020861687 scopus 로고
    • Water and proteins : II. The location and dynamics of water in protein systems and its relation to their stability and properties
    • [11] J.T. Edsall, H.A. McKenzie, Water and proteins : II. The location and dynamics of water in protein systems and its relation to their stability and properties, Adv. Biophys. 16 (1983) 53-183.
    • (1983) Adv. Biophys. , vol.16 , pp. 53-183
    • Edsall, J.T.1    McKenzie, H.A.2
  • 12
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvoluted FTIR spectra
    • [12] D.M. Byler, H. Susi, Examination of the secondary structure of proteins by deconvoluted FTIR spectra, Biopolymers 25 (1986) 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 13
    • 0022463740 scopus 로고
    • Resolution enhanced Fourier transform infrared spectroscopy of enzymes
    • [13] H. Susi, D.M. Byler, Resolution enhanced Fourier transform infrared spectroscopy of enzymes, Methods Enzymol. 130 (1986) 290-311.
    • (1986) Methods Enzymol. , vol.130 , pp. 290-311
    • Susi, H.1    Byler, D.M.2
  • 14
    • 0023837785 scopus 로고
    • New insights into protein conformation from infrared spectroscopy
    • [14] W.K. Surewicz, H.H. Mantsch, New insights into protein conformation from infrared spectroscopy, Biochim. Biophys. Acta 953 (1988) 115-130.
    • (1988) Biochim. Biophys. Acta , vol.953 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 15
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides and proteins
    • [15] S. Krimm, J. Bandekar, Vibrational spectroscopy and conformation of peptides, polypeptides and proteins, Adv. Protein Chem. 38 (1986) 181-364.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 16
    • 0028307232 scopus 로고
    • Infrared methods for study of hemoglobin reactions and structures
    • [16] A. Dong, W.S. Caughey, Infrared methods for study of hemoglobin reactions and structures, Methods Enzymol. 232 (1994) 139-175.
    • (1994) Methods Enzymol. , vol.232 , pp. 139-175
    • Dong, A.1    Caughey, W.S.2
  • 18
    • 0030059491 scopus 로고    scopus 로고
    • Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine structural similarity of a protein in different states
    • [18] B.S. Kendrick, A. Dong, S.D. Allison, M.C. Manning, J.F. Carpenter, Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine structural similarity of a protein in different states, J. Pharm. Sci. 85 (1996) 155-158.
    • (1996) J. Pharm. Sci. , vol.85 , pp. 155-158
    • Kendrick, B.S.1    Dong, A.2    Allison, S.D.3    Manning, M.C.4    Carpenter, J.F.5
  • 19
    • 0030443488 scopus 로고    scopus 로고
    • Effect of polymer liquid-liquid phase separation on hemoglobin structure during freeze-drying
    • [19] M. Heller, J.F. Carpenter, T.W. Randolph, Effect of polymer liquid-liquid phase separation on hemoglobin structure during freeze-drying, J. Pharm. Sci. 85 (1996) 1358-1362.
    • (1996) J. Pharm. Sci. , vol.85 , pp. 1358-1362
    • Heller, M.1    Carpenter, J.F.2    Randolph, T.W.3
  • 20
    • 0030041320 scopus 로고    scopus 로고
    • Infrared and circular dichroism spectroscopic characterization of structural differences between β-lactoglobulin A and B
    • [20] A. Dong, J. Matsuura, S.D. Allison, E. Chrisman, M.C. Manning, J.F. Carpenter, Infrared and circular dichroism spectroscopic characterization of structural differences between β-lactoglobulin A and B, Biochemistry 35 (1996) 1450-1457.
    • (1996) Biochemistry , vol.35 , pp. 1450-1457
    • Dong, A.1    Matsuura, J.2    Allison, S.D.3    Chrisman, E.4    Manning, M.C.5    Carpenter, J.F.6
  • 21
    • 0009071257 scopus 로고
    • Formation of glasses from liquids and biopolymers
    • [21] C.A. Angell, Formation of glasses from liquids and biopolymers, Science 267 (1995) 1924-1935.
    • (1995) Science , vol.267 , pp. 1924-1935
    • Angell, C.A.1
  • 22
    • 0025801181 scopus 로고
    • The effects of additives on the stability of freeze-dried β-galactosidase stored at elevated temperatures
    • [22] K. Izutsu, S. Yoshioka, Y. Takeda, The effects of additives on the stability of freeze-dried β-galactosidase stored at elevated temperatures, Int. J. Pharm. 71 (1991) 137-146.
    • (1991) Int. J. Pharm. , vol.71 , pp. 137-146
    • Izutsu, K.1    Yoshioka, S.2    Takeda, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.