메뉴 건너뛰기




Volumn 25, Issue 2, 2008, Pages 259-267

Effects of excipients on protein conformation in lyophilized solids by hydrogen/deuterium exchange mass spectrometry

Author keywords

ESI mass spectrometry; Excipient; FTIR; Hydrogen deuterium exchange; Lyophilization; Protein

Indexed keywords

CALMODULIN; DEXTRAN 12000; DEXTRAN 5000; EXCIPIENT; GUANIDINE; MANNITOL; RAFFINOSE; SUCROSE; UNCLASSIFIED DRUG;

EID: 39149141888     PISSN: 07248741     EISSN: 1573904X     Source Type: Journal    
DOI: 10.1007/s11095-007-9365-6     Document Type: Article
Times cited : (43)

References (23)
  • 1
    • 33645170297 scopus 로고    scopus 로고
    • Excipients for use in lyophilized pharmaceutical peptide, protein, and other bioproducts
    • H. R. Costantino. Excipients for use in lyophilized pharmaceutical peptide, protein, and other bioproducts. Biotechnology: Pharmaceutical Aspects 2:139-228 (2004).
    • (2004) Biotechnology: Pharmaceutical Aspects , vol.2 , pp. 139-228
    • Costantino, H.R.1
  • 2
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation
    • A. Dong, S. J. Prestrelski, S. D. Allison, and J. F. Carpenter. Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. J. Pharm. Sci. 84:415-424 (1995).
    • (1995) J. Pharm. Sci. , vol.84 , pp. 415-424
    • Dong, A.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 3
    • 0030059491 scopus 로고    scopus 로고
    • Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states
    • B. S. Kendrick, A. Dong, S. D. Allison, M. C. Manning, and J. F. Carpenter. 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 (1996).
    • (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
  • 5
    • 0037308304 scopus 로고    scopus 로고
    • Effects of types of sugar on the stabilization of protein in the dried state
    • K. Imamura, T. Ogawa, T. Sakiyama, and K. Nakanishi. Effects of types of sugar on the stabilization of protein in the dried state. J. Pharm. Sci. 92:266-274 (2003).
    • (2003) J. Pharm. Sci. , vol.92 , pp. 266-274
    • Imamura, K.1    Ogawa, T.2    Sakiyama, T.3    Nakanishi, K.4
  • 6
    • 1542275162 scopus 로고    scopus 로고
    • Protection of protein secondary structure by saccharides of different molecular weights during freeze-drying
    • K.-I. Izutsu, N. Aoyagi, and S. Kojima. Protection of protein secondary structure by saccharides of different molecular weights during freeze-drying. Chem. Pharm. Bull. 52:199-203 (2004).
    • (2004) Chem. Pharm. Bull. , vol.52 , pp. 199-203
    • Izutsu, K.-I.1    Aoyagi, N.2    Kojima, S.3
  • 7
    • 55449104956 scopus 로고    scopus 로고
    • Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations
    • J. D. Andya, C. C. Hsu, and S. J. Shire. Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations. PharmSci. 5:E10 (2003).
    • (2003) PharmSci. , vol.5 , pp. 10
    • Andya, J.D.1    Hsu, C.C.2    Shire, S.J.3
  • 8
    • 0033562141 scopus 로고    scopus 로고
    • Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding
    • S. D. Allison, B. Chang, T. W. Randolph, and J. F. Carpenter. Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding. Arch. Biochem. Biophys. 365:289-298 (1999).
    • (1999) Arch. Biochem. Biophys. , vol.365 , pp. 289-298
    • Allison, S.D.1    Chang, B.2    Randolph, T.W.3    Carpenter, J.F.4
  • 9
    • 34248566786 scopus 로고    scopus 로고
    • Characterizing protein structure in amorphous solids using hydrogen/deuterium exchange with mass spectrometry
    • Y. Li, T. D. Williams, R. L. Schowen, and E. M. Topp. Characterizing protein structure in amorphous solids using hydrogen/deuterium exchange with mass spectrometry. Anal. Biochem. 366:18-28.
    • Anal. Biochem. , vol.366 , pp. 18-28
    • Li, Y.1    Williams, T.D.2    Schowen, R.L.3    Topp, E.M.4
  • 10
    • 0003127079 scopus 로고
    • Saturated salt solutions for maintaining specified relative humidities
    • H. Nyqvist. Saturated salt solutions for maintaining specified relative humidities. Int. J. Pharm. Technol. Prod. Manuf. 4:47-48 (1983).
    • (1983) Int. J. Pharm. Technol. Prod. Manuf. , vol.4 , pp. 47-48
    • Nyqvist, H.1
  • 11
    • 0346431875 scopus 로고    scopus 로고
    • Probing Ca2+-induced conformational changes in porcine calmodulin by H/D exchange and ESI-MS: Effect of cations and ionic strength
    • M. M. Zhu, D. L. Rempel, J. Zhao, D. E. Giblin, and M. L. Gross. Probing Ca2+-induced conformational changes in porcine calmodulin by H/D exchange and ESI-MS: Effect of cations and ionic strength. Biochemistry 42:15388-15397 (2003).
    • (2003) Biochemistry , vol.42 , pp. 15388-15397
    • Zhu, M.M.1    Rempel, D.L.2    Zhao, J.3    Giblin, D.E.4    Gross, M.L.5
  • 12
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Z. Zhang, and D. L. Smith. Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation. Protein Sci. 2:522-531 (1993).
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 13
    • 0033044298 scopus 로고    scopus 로고
    • The effect of temperature on water vapor sorption by some amorphous pharmaceutical sugars
    • B. C. Hancock, and C. R. Dalton. The effect of temperature on water vapor sorption by some amorphous pharmaceutical sugars. Pharm. Dev. Technol. 4:125-131 (1999).
    • (1999) Pharm. Dev. Technol. , vol.4 , pp. 125-131
    • Hancock, B.C.1    Dalton, C.R.2
  • 14
    • 0035994868 scopus 로고    scopus 로고
    • Excipient crystallinity and its protein-structure-stabilizing effect during freeze-drying
    • K.-I. Izutsu, and S. Kojima. Excipient crystallinity and its protein-structure-stabilizing effect during freeze-drying. J. Pharm. Pharmacol. 54:1033-1039 (2002).
    • (2002) J. Pharm. Pharmacol. , vol.54 , pp. 1033-1039
    • Izutsu, K.-I.1    Kojima, S.2
  • 15
    • 25444524564 scopus 로고    scopus 로고
    • Effects of sucrose and mannitol on asparagine deamidation rates of model peptides in solution and in the solid state
    • B. Li, M. H. O'Meara, J. W. Lubach, R. L. Schowen, E. M. Topp, E. J. Munson, and R. T. Borchardt. 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).
    • (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
  • 17
    • 0026046615 scopus 로고
    • Fourier transform infrared spectroscopic studies of calcium-binding proteins
    • M. Jackson, P. I. Haris, and D. Chapman. Fourier transform infrared spectroscopic studies of calcium-binding proteins. Biochemistry 30:9681-9686 (1991).
    • (1991) Biochemistry , vol.30 , pp. 9681-9686
    • Jackson, M.1    Haris, P.I.2    Chapman, D.3
  • 18
    • 0024583565 scopus 로고
    • Calmodulin and troponin C structures studied by Fourier transform infrared spectroscopy: Effects of calcium and magnesium binding
    • J. Trewhella, W. K. Liddle, D. B. Heidorn, and N. Strynadka. Calmodulin and troponin C structures studied by Fourier transform infrared spectroscopy: effects of calcium and magnesium binding. Biochemistry 28:1294-1301 (1989).
    • (1989) Biochemistry , vol.28 , pp. 1294-1301
    • Trewhella, J.1    Liddle, W.K.2    Heidorn, D.B.3    Strynadka, N.4
  • 19
    • 0024549238 scopus 로고
    • An infrared spectroscopic study of the interactions of carbohydrates with dried proteins
    • J. F. Carpenter, and J. H. Crowe. An infrared spectroscopic study of the interactions of carbohydrates with dried proteins. Biochemistry. 28:3916-3922 (1989).
    • (1989) Biochemistry , vol.28 , pp. 3916-3922
    • Carpenter, J.F.1    Crowe, J.H.2
  • 20
    • 0037016451 scopus 로고    scopus 로고
    • The hydrogen bond in the solid state
    • T. Steiner. The hydrogen bond in the solid state. Angew. Chem., Int. Ed. Engl. 41:48-76 (2002).
    • (2002) Angew. Chem., Int. Ed. Engl. , vol.41 , pp. 48-76
    • Steiner, T.1
  • 21
    • 0025875873 scopus 로고
    • Occurrence of bifurcated three-center hydrogen bonds in proteins
    • R. Preissner, U. Egner, and W. Saenger. Occurrence of bifurcated three-center hydrogen bonds in proteins. FEBS Lett. 288:192-196 (1991).
    • (1991) FEBS Lett. , vol.288 , pp. 192-196
    • Preissner, R.1    Egner, U.2    Saenger, W.3
  • 22
    • 3242688589 scopus 로고    scopus 로고
    • Bifurcated hydrogen bonds: Three-centered interactions
    • I. Rozas, I. Alkorta, and J. Elguero. Bifurcated hydrogen bonds: three-centered interactions. J. Phys. Chem. A. 102:9925-9932 (1998).
    • (1998) J. Phys. Chem. A. , vol.102 , pp. 9925-9932
    • Rozas, I.1    Alkorta, I.2    Elguero, J.3
  • 23
    • 33745926621 scopus 로고    scopus 로고
    • Freezing- and drying-induced perturbations of protein structure and mechanisms of protein protection by stabilizing additives
    • J. F. Carpenter, K.-I. Izutsu, and T. W. Randolph. Freezing- and drying-induced perturbations of protein structure and mechanisms of protein protection by stabilizing additives. Drugs Pharm. Sci. 137:147-186 (2004).
    • (2004) Drugs Pharm. Sci. , vol.137 , pp. 147-186
    • Carpenter, J.F.1    Izutsu, K.-I.2    Randolph, T.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.