메뉴 건너뛰기




Volumn 95, Issue 4, 2006, Pages 781-789

Near-infrared analysis of protein secondary structure in aqueous solutions and freeze-dried solids

Author keywords

Freeze drying; Near infrared spectroscopy; Protein formulation; Protein structure; Stability

Indexed keywords

BETA LACTOGLOBULIN; BOVINE SERUM ALBUMIN; CYTOCHROME C; IMMUNOGLOBULIN; MYOGLOBIN; OVALBUMIN;

EID: 33645980951     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.20580     Document Type: Article
Times cited : (66)

References (42)
  • 3
    • 28244432903 scopus 로고    scopus 로고
    • Costantino HR, Pikal MJ, editors. Arlington: American Association of Pharmaceutical Scientists
    • Costantino HR, Pikal MJ, editors. 2004. Lyophilization of biopharmaceuticals. Arlington: American Association of Pharmaceutical Scientists.
    • (2004) Lyophilization of Biopharmaceuticals
  • 4
    • 0030586287 scopus 로고    scopus 로고
    • Physical factors affecting the storage stability of freeze-dried interleukin-1 receptor antagonist: Glass transition and protein conformation
    • Chang BS, Beauvais RM, Dong A, Carpenter JF. 1996. Physical factors affecting the storage stability of freeze-dried interleukin-1 receptor antagonist: Glass transition and protein conformation. Arch Biochem Biophys 331:249-258.
    • (1996) Arch Biochem Biophys , vol.331 , pp. 249-258
    • Chang, B.S.1    Beauvais, R.M.2    Dong, A.3    Carpenter, J.F.4
  • 5
    • 25444524564 scopus 로고    scopus 로고
    • Effects of sucrose and mannitol on asparagine deamidation rates of model peptides in solution and in the solid state
    • Li B, O'meara MH, Lubach JW, Schowen RL, Topp EM, Munson EJ, Borchardt RT. 2005. Effects of sucrose and mannitol on asparagine deamidation rates of model peptides in solution and in the solid state. J Pharm Sci 94:1723-1735.
    • (2005) J Pharm Sci , vol.94 , pp. 1723-1735
    • Li, B.1    O'Meara, M.H.2    Lubach, J.W.3    Schowen, R.L.4    Topp, E.M.5    Munson, E.J.6    Borchardt, R.T.7
  • 6
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation
    • 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.
    • (1995) J Pharm Sci , vol.84 , pp. 415-424
    • Dong, A.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 7
    • 0027176042 scopus 로고
    • Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization. II. Structural studies using infrared spectroscopy
    • 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 303:465-473.
    • (1993) Arch Biochem Biophys , vol.303 , pp. 465-473
    • Prestrelski, S.J.1    Arakawa, T.2    Carpenter, J.F.3
  • 8
    • 0037139368 scopus 로고    scopus 로고
    • Investigation of protein/carbohydrate interactions in the dried state. 2. Diffuse reflectance FTIR studies
    • 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.
    • (2002) Int J Pharm , vol.235 , pp. 207-218
    • Souillac, P.O.1    Middaugh, C.R.2    Rytting, J.H.3
  • 11
    • 0030028852 scopus 로고    scopus 로고
    • Aggregation of rhDNase occurred during the compression of KBr pellets used for FTIR spectroscopy
    • 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.
    • (1996) Pharm Res , vol.13 , pp. 238-242
    • Chan, H.K.1    Ongpipattanakul, B.2    Au-Yeung, J.3
  • 12
    • 0035887070 scopus 로고    scopus 로고
    • Fourier transform infrared spectrometric analysis of protein conformation: Effect of sampling method and stress factors
    • van de Weert M, Haris PI, Hennink WE, Crommelin DJ. 2001. Fourier transform infrared spectrometric analysis of protein conformation: Effect of sampling method and stress factors. Anal Biochem 297:160-169.
    • (2001) Anal Biochem , vol.297 , pp. 160-169
    • Van De Weert, M.1    Haris, P.I.2    Hennink, W.E.3    Crommelin, D.J.4
  • 13
    • 0024845319 scopus 로고
    • Near-infrared spectroscopic determination of residual moisture in lyophilized sucrose through intact glass vials
    • Kamat MS, Lodder RA, DeLuca PP. 1989. Near-infrared spectroscopic determination of residual moisture in lyophilized sucrose through intact glass vials. Pharm Res 6:961-965.
    • (1989) Pharm Res , vol.6 , pp. 961-965
    • Kamat, M.S.1    Lodder, R.A.2    DeLuca, P.P.3
  • 14
    • 0031786396 scopus 로고    scopus 로고
    • Determination of adequate moisture content for efficient dry-heat viral inactivation in lyophilized factor VIII by loss on drying and by near infrared spectroscopy
    • Savage M, Torres J, Franks L, Masecar B, Hotta J. 1998. Determination of adequate moisture content for efficient dry-heat viral inactivation in lyophilized factor VIII by loss on drying and by near infrared spectroscopy. Biologicals 26:119-124.
    • (1998) Biologicals , vol.26 , pp. 119-124
    • Savage, M.1    Torres, J.2    Franks, L.3    Masecar, B.4    Hotta, J.5
  • 16
    • 24044452577 scopus 로고    scopus 로고
    • Effect of counterions on the physical properties of L-arginine in frozen solutions and freeze-dried solids
    • Izutsu K, Fujimaki Y, Kuwabara A, Aoyagi N. 2005. Effect of counterions on the physical properties of L-arginine in frozen solutions and freeze-dried solids. Int J Pharm 301:161-169.
    • (2005) Int J Pharm , vol.301 , pp. 161-169
    • Izutsu, K.1    Fujimaki, Y.2    Kuwabara, A.3    Aoyagi, N.4
  • 17
    • 27644477359 scopus 로고    scopus 로고
    • Noninvasive determination of protein conformation in the solid state using near infrared (NIR) spectroscopy
    • Bai S, Nayar R, Carpenter JF, Manning MC. 2005. Noninvasive determination of protein conformation in the solid state using near infrared (NIR) spectroscopy. J Pharm Sci 94:2030-2038.
    • (2005) J Pharm Sci , vol.94 , pp. 2030-2038
    • Bai, S.1    Nayar, R.2    Carpenter, J.F.3    Manning, M.C.4
  • 19
    • 0033075461 scopus 로고    scopus 로고
    • Monitoring the secondary structure of proteins by near-infrared spectroscopy
    • Robert P, Devaux MF, Mouhous N, Dufour E. 1999. Monitoring the secondary structure of proteins by near-infrared spectroscopy. Appl Spectrosc 53:226-232.
    • (1999) Appl Spectrosc , vol.53 , pp. 226-232
    • Robert, P.1    Devaux, M.F.2    Mouhous, N.3    Dufour, E.4
  • 20
    • 0001746515 scopus 로고    scopus 로고
    • Second derivative near infrared studies on the structural characterisation of proteins
    • Miyazawa M, Sonoyama M. 1998. Second derivative near infrared studies on the structural characterisation of proteins. J Near Infrared Spectrosc 6:253-257.
    • (1998) J Near Infrared Spectrosc , vol.6 , pp. 253-257
    • Miyazawa, M.1    Sonoyama, M.2
  • 21
    • 0033700031 scopus 로고    scopus 로고
    • Two-dimensional near-infrared spectroscopy study of human serum albumin in aqueous solutions: Using overtones and combination modes to monitor temperature-dependent changes in the secondary structure
    • Wu Y, Czarnik-Matusewicz B, Murayama K, Ozaki Y. 2000. Two-dimensional near-infrared spectroscopy study of human serum albumin in aqueous solutions: Using overtones and combination modes to monitor temperature-dependent changes in the secondary structure. J Phys Chem B 104:5840-5847.
    • (2000) J Phys Chem B , vol.104 , pp. 5840-5847
    • Wu, Y.1    Czarnik-Matusewicz, B.2    Murayama, K.3    Ozaki, Y.4
  • 22
    • 0142135858 scopus 로고    scopus 로고
    • Modeling temperature-dependent protein structural transitions by combined near-IR and mid-IR spectroscopies and multivariate curve resolution
    • Navea S, de Juan A, Tauler R. 2003. Modeling temperature-dependent protein structural transitions by combined near-IR and mid-IR spectroscopies and multivariate curve resolution. Anal Chem 75:5592-5601.
    • (2003) Anal Chem , vol.75 , pp. 5592-5601
    • Navea, S.1    De Juan, A.2    Tauler, R.3
  • 23
    • 0009960298 scopus 로고
    • The applicability of near-infrared reflectance spectroscopy for determining solubility and digestability of heated protein under high pressure
    • Cho RK, Lee JH, Ahn JJ, Ozaki Y, Iwamoto M. 1995. The applicability of near-infrared reflectance spectroscopy for determining solubility and digestability of heated protein under high pressure. J Near Infrared Spectrosc 3:73-79.
    • (1995) J Near Infrared Spectrosc , vol.3 , pp. 73-79
    • Cho, R.K.1    Lee, J.H.2    Ahn, J.J.3    Ozaki, Y.4    Iwamoto, M.5
  • 24
    • 0035994868 scopus 로고    scopus 로고
    • Excipient crystallinity and its protein structure-stabilizing effect during freeze-drying
    • Izutsu K, Kojima S. 2002. Excipient crystallinity and its protein structure-stabilizing effect during freeze-drying. J Pharm Pharmacol 54:1033-1039.
    • (2002) J Pharm Pharmacol , vol.54 , pp. 1033-1039
    • Izutsu, K.1    Kojima, S.2
  • 25
    • 0013125585 scopus 로고    scopus 로고
    • Application of NIR spectroscopy to agricultural products
    • Burns DA, Ciurczak EW, editors New York: Marcel Dekker
    • Shenk JS, Jerome J, Workman J, Westerhaus MO. 2001. Application of NIR spectroscopy to agricultural products. In: Burns DA, Ciurczak EW, editors Handbook of Near-infrared Analysis. New York: Marcel Dekker. pp 419-471.
    • (2001) Handbook of Near-Infrared Analysis , pp. 419-471
    • Shenk, J.S.1    Jerome, J.2    Workman, J.3    Westerhaus, M.O.4
  • 26
    • 0034225076 scopus 로고    scopus 로고
    • Comparison between conventional spectral analysis methods, chemometrics, and two-dimensional correlation spectroscopy in the analysis of near-infrared spectra of protein
    • Murayama K, Czarnik-Matusewicz B, Wu Y, Tsenkova R, Ozaki Y. 2000. Comparison between conventional spectral analysis methods, chemometrics, and two-dimensional correlation spectroscopy in the analysis of near-infrared spectra of protein. Appl Spectrosc 54:978-985.
    • (2000) Appl Spectrosc , vol.54 , pp. 978-985
    • Murayama, K.1    Czarnik-Matusewicz, B.2    Wu, Y.3    Tsenkova, R.4    Ozaki, Y.5
  • 27
    • 33751157473 scopus 로고
    • Photoacoustic near-infrared investigation of homopolypeptides
    • Wang J, Sowa MG, Ahmed MK, Mantsch HH. 1994. Photoacoustic near-infrared investigation of homopolypeptides. J Phys Chem 98:4748-4755.
    • (1994) J Phys Chem , vol.98 , pp. 4748-4755
    • Wang, J.1    Sowa, M.G.2    Ahmed, M.K.3    Mantsch, H.H.4
  • 28
    • 0242306126 scopus 로고    scopus 로고
    • Temperature-dependent near-infrared spectra of bovine serum albumin in aqueous solutions: Spectral analysis by principal component analysis and evolving factor analysis
    • Yuan B, Murayama K, Wu Y, Tsenkova R, Dou X, Era S, Ozaki Y. 2003. Temperature-dependent near-infrared spectra of bovine serum albumin in aqueous solutions: Spectral analysis by principal component analysis and evolving factor analysis. Appl Spectrosc 57:1223-1229.
    • (2003) Appl Spectrosc , vol.57 , pp. 1223-1229
    • Yuan, B.1    Murayama, K.2    Wu, Y.3    Tsenkova, R.4    Dou, X.5    Era, S.6    Ozaki, Y.7
  • 29
    • 0018814387 scopus 로고
    • A near-infrared analysis of water-macromolecule interactions: Hydration and the spectra of aqueous solutions of intact proteins
    • Vandermeulen DL, Ressler N. 1980. A near-infrared analysis of water-macromolecule interactions: Hydration and the spectra of aqueous solutions of intact proteins. Arch Biochem Biophys 199:197-205.
    • (1980) Arch Biochem Biophys , vol.199 , pp. 197-205
    • Vandermeulen, D.L.1    Ressler, N.2
  • 30
    • 0032487372 scopus 로고    scopus 로고
    • Measurement of glucose and other analytes in undiluted human serum with near-infrared transmission spectroscopy
    • Hazen KH, Arnold MA, Small GW. 1998. Measurement of glucose and other analytes in undiluted human serum with near-infrared transmission spectroscopy. Anal Chim Acta 371:255-267.
    • (1998) Anal Chim Acta , vol.371 , pp. 255-267
    • Hazen, K.H.1    Arnold, M.A.2    Small, G.W.3
  • 32
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • Dong A, Huang P, Caughey WS. 1990. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29:3303-3308.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 33
    • 4444344985 scopus 로고    scopus 로고
    • Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier transform infrared spectroscopy
    • Murayama K, Tomida M. 2004. Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier transform infrared spectroscopy. Biochemistry 43:11526-11532.
    • (2004) Biochemistry , vol.43 , pp. 11526-11532
    • Murayama, K.1    Tomida, M.2
  • 35
    • 0029148319 scopus 로고
    • Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis
    • van Stokkum IH, Linsdell H, Hadden JM, Haris PI, Chapman D, Bloemendal M. 1995. Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis. Biochemistry 34:10508-10518.
    • (1995) Biochemistry , vol.34 , pp. 10508-10518
    • Van Stokkum, I.H.1    Linsdell, H.2    Hadden, J.M.3    Haris, P.I.4    Chapman, D.5    Bloemendal, M.6
  • 36
    • 0006454079 scopus 로고
    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • Buchner J, Rudolph R. 1991. Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Biotechnology (N Y) 9:157-162.
    • (1991) Biotechnology (N Y) , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 37
    • 0028529836 scopus 로고
    • Studies on spectra/structure correlations in near-infrared spectra of proteins and polypeptides. Part I: A marker band for hydrogen bonds
    • Liu Y, Cho R-K, Sakuri K, Miura T, Ozaki Y. 1994. Studies on spectra/structure correlations in near-infrared spectra of proteins and polypeptides. Part I: A marker band for hydrogen bonds. Appl Spectrosc 48:1249-12554.
    • (1994) Appl Spectrosc , vol.48 , pp. 1249-12554
    • Liu, Y.1    Cho, R.-K.2    Sakuri, K.3    Miura, T.4    Ozaki, Y.5
  • 38
    • 0022825987 scopus 로고
    • Calculation of the partial specific volumes of proteins in concentrated salt, sugar, and amino acid solutions
    • Arakawa T. 1986. Calculation of the partial specific volumes of proteins in concentrated salt, sugar, and amino acid solutions. J Biochem 100:1471-1475.
    • (1986) J Biochem , vol.100 , pp. 1471-1475
    • Arakawa, T.1
  • 39
    • 0344845411 scopus 로고    scopus 로고
    • Effects of disulfide bonds on compactness of protein molecules revealed by volume, compressibility, and expansibility changes during reduction
    • Gekko K, Kimoto A, Kamiyama T. 2003. Effects of disulfide bonds on compactness of protein molecules revealed by volume, compressibility, and expansibility changes during reduction. Biochemistry 42:13746-13753.
    • (2003) Biochemistry , vol.42 , pp. 13746-13753
    • Gekko, K.1    Kimoto, A.2    Kamiyama, T.3
  • 40
    • 0000045935 scopus 로고    scopus 로고
    • Determination of human serum albumin and γ-globulin in a control serum solution by near-infrared spectroscopy and partial least squares regression
    • Murayama K, Yamada K, Tsenkova R, Wang Y, Ozaki Y. 1998. Determination of human serum albumin and γ-globulin in a control serum solution by near-infrared spectroscopy and partial least squares regression. Fresenius J Anal Chem 362:155-166.
    • (1998) Fresenius J Anal Chem , vol.362 , pp. 155-166
    • Murayama, K.1    Yamada, K.2    Tsenkova, R.3    Wang, Y.4    Ozaki, Y.5
  • 41
    • 33645959045 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy
    • Jiskoot W, Crommelin D, editors. Arlington: American Association of Pharmaceutical Scientists
    • van de Weert M, Hering JA, Haris PI. 2005. Fourier transform infrared spectroscopy. In: Jiskoot W, Crommelin D, editors. Methods for structural analysis of protein pharmaceuticals. Arlington: American Association of Pharmaceutical Scientists. pp 131-166.
    • (2005) Methods for Structural Analysis of Protein Pharmaceuticals , pp. 131-166
    • Van De Weert, M.1    Hering, J.A.2    Haris, P.I.3
  • 42
    • 0037335194 scopus 로고    scopus 로고
    • In-situ near-infrared spectroscopy monitoring of the lyophilization process
    • Brulls M, Folestad S, Sparen A, Rasmuson A. 2003. In-situ near-infrared spectroscopy monitoring of the lyophilization process. Pharm Res 20:494-499.
    • (2003) Pharm Res , vol.20 , pp. 494-499
    • Brulls, M.1    Folestad, S.2    Sparen, A.3    Rasmuson, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.