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Volumn 17, Issue 3, 2012, Pages

Breaking old habits: Moving away from commonly used buffers in pharmaceuticals

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; ASPARTIC ACID; BUFFER; CITRIC ACID; EXCIPIENT; FUMARIC ACID; HISTIDINE; LACTIC ACID; MALIC ACID; PHOSPHORIC ACID; SODIUM DIHYDROGEN PHOSPHATE; SUCCINIC ACID; TROMETAMOL;

EID: 84877000615     PISSN: 13608606     EISSN: None     Source Type: Trade Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (42)
  • 3
    • 75349114023 scopus 로고    scopus 로고
    • Recent trends in stabilising peptides and proteins in pharmaceutical formulation - Considerations in the choice of excipients
    • Jorgensen, L, Hostrup, S., Moeller, E. H., Grohganz H. (2009) Recent Trends in Stabilising Peptides and Proteins in Pharmaceutical Formulation - Considerations in the Choice of Excipients. Expert Opinion. 6, 1219-1230
    • (2009) Expert Opinion. , vol.6 , pp. 1219-2123
    • Jorgensen, L.1    Hostrup, S.2    Moeller, E.H.3    Grohganz, H.4
  • 4
    • 80054717076 scopus 로고    scopus 로고
    • Protein-excipient interactions: Mechanisms and biophysical characterization applied to protein formulation development
    • Kamerzell, T. J., Esfandiary, R, Joshi, S. B., Middaugh, C. R, Volkin, D. B. (2011) Protein-Excipient Interactions: Mechanisms and Biophysical Characterization Applied to Protein Formulation Development. Adv. Drug Delivery Reviews. 63, 1118-1159
    • (2011) Adv. Drug Delivery Reviews. , vol.63 , pp. 1118-1159
    • Kamerzell, T.J.1    Esfandiary, R.2    Joshi, S.B.3    Middaugh, C.R.4    Volkin, D.B.5
  • 6
    • 55749096388 scopus 로고    scopus 로고
    • Measuring and increasing protein solubility
    • Trevino, S. R., Scholtz, J. M., Pace, C. N. (2008) Measuring and Increasing Protein Solubility. J. Pharm. Sci. 97, 4155-4166
    • (2008) J. Pharm. Sci. , vol.97 , pp. 4155-4166
    • Trevino, S.R.1    Scholtz, J.M.2    Pace, C.N.3
  • 7
    • 77951498805 scopus 로고    scopus 로고
    • Protein aggregation-pathways and influencing factors
    • Wang, W., Nema, S., Teagarden, D. (2010) Protein Aggregation-Pathways and Influencing Factors. Int. J. Pharmaceutics. 390, 89-99
    • (2010) Int. J. Pharmaceutics. , vol.390 , pp. 89-99
    • Wang, W.1    Nema, S.2    Teagarden, D.3
  • 8
    • 0017666980 scopus 로고
    • Changes in apparent ph on freezing aqueous buffer solutions and their relevance to biochemical electron-paramagnetic-resonance spectroscopy
    • Williams-Smith, D. (1977) Changes in Apparent pH on Freezing Aqueous Buffer Solutions and their Relevance to Biochemical Electron-Paramagnetic- Resonance Spectroscopy. Biochem. J. 167, 593-600.
    • (1977) Biochem. J. , vol.167 , pp. 593-600
    • Williams-Smith, D.1
  • 9
    • 77954700033 scopus 로고    scopus 로고
    • Impact of freezing on ph of buffered solutions and consequences for monoclonal antibody aggregation
    • Kolhe, P., Amend, E., Singh, S. K. (2010) Impact of Freezing on pH of Buffered Solutions and Consequences for Monoclonal Antibody Aggregation. Biotechnol. Prog. 26, 727-733
    • (2010) Biotechnol. Prog. , vol.26 , pp. 727-733
    • Kolhe, P.1    Amend, E.2    Singh, S.K.3
  • 10
    • 0035054119 scopus 로고    scopus 로고
    • Effect of initial buffer composition on ph changes during far-from-equilibrium freezing of sodium phosphate buffer solutions
    • Gomez, G., Pikal, M. J., Rodriguez-Homedo, N. (2001) Effect of Initial Buffer Composition on pH Changes during Far-From-Equilibrium Freezing of Sodium Phosphate Buffer Solutions. Pharm. Res. 18, 90-97
    • (2001) Pharm. Res. , vol.18 , pp. 90-97
    • Gomez, G.1    Pikal, M.J.2    Rodriguez-Homedo, N.3
  • 11
    • 0024456040 scopus 로고
    • The cold-induced denaturation of lactate dehydrogenase at sub-zero temperatures in the absence of perturbants
    • Hatley R.H.M., Franks, F. (1989) The Cold-Induced Denaturation of Lactate Dehydrogenase at Sub-Zero Temperatures in the Absence of Perturbants. FEBS Lett 257,171-173
    • (1989) FEBS Lett , vol.257 , pp. 171-173
    • Hatley, R.H.M.1    Franks, F.2
  • 12
    • 0033817986 scopus 로고    scopus 로고
    • Solid-state chemistry of a novel carbapenem with a releasable sidechain
    • Almarsson, O., Seburg, R.A., Godshall, D., Tsai, E. W., Kaufman, M. J. (2000), Solid-State Chemistry of a Novel Carbapenem with a Releasable Sidechain, Tetrahedron 56, 6877-6885
    • (2000) Tetrahedron , vol.56 , pp. 6877-6885
    • Almarsson, O.1    Seburg, R.A.2    Godshall, D.3    Tsai, E.W.4    Kaufman, M.J.5
  • 13
    • 0030604045 scopus 로고    scopus 로고
    • Replacing succinate with glycolate buffer improves the stability of lyophilized interferongamma
    • Lam, X M., Costantino, H. R, Overcashier, D. E., Nguyen, T. H., and Hsu, C. C. (1996) Replacing Succinate with Glycolate Buffer Improves the Stability of Lyophilized Interferongamma. Int. J. Pharm. 142, 85-95
    • (1996) Int. J. Pharm. , vol.142 , pp. 85-95
    • Lam, X.M.1    Costantino, H.R.2    Overcashier, D.E.3    Nguyen, T.H.4    Hsu, C.C.5
  • 14
    • 84985222661 scopus 로고
    • Aspartame degradation kinetics as affected by ph in intermediate and low moisture food systems
    • Bell, L.N., Labuza, T.P. (1991) Aspartame Degradation Kinetics as Affected by pH in Intermediate and Low Moisture Food Systems, J. Food Sci. 56, 17-20
    • (1991) J. Food Sci. , vol.56 , pp. 17-22
    • Bell, L.N.1    Labuza, T.P.2
  • 15
    • 0032703669 scopus 로고    scopus 로고
    • Effects of buffer composition and processing conditions on aggregation of bovine igg during freeze-drying
    • Sarciaux, J.M., Mansour, S., Hageman, M.J., Nail, S.L. (1999) Effects of Buffer Composition and Processing Conditions on Aggregation of Bovine IgG during Freeze-Drying, J. Pharm. Sci. 88, 1354-1361
    • (1999) J. Pharm. Sci. , vol.88 , pp. 1354-1361
    • Sarciaux, J.M.1    Mansour, S.2    Hageman, M.J.3    Nail, S.L.4
  • 16
    • 0034833878 scopus 로고    scopus 로고
    • Lyophilization- induced protein denaturation in phosphate buffer systems: Monomelic and tetrameric b-galactosidase
    • Pikal-Cleland, K.A., Carpenter, J.F. (2001) Lyophilization- Induced Protein Denaturation in Phosphate Buffer Systems: Monomelic and Tetrameric b-galactosidase, J. Pharm. Sci. 90, 1255-1268
    • (2001) J. Pharm. Sci. , vol.90 , pp. 1255-1268
    • Pikal-Cleland, K.A.1    Carpenter, J.F.2
  • 17
    • 84876984379 scopus 로고    scopus 로고
    • The impact of buffer on solid-state properties and stability of freeze-dried dosage forms
    • (eds F. Jameel and S. Hershenson), John Wiley & Sons, Inc., Hoboken, NJ, USA
    • Shalaev, E.Y., Gatlin, L.A. (2010) The Impact of Buffer on Solid-State Properties and Stability of Freeze-Dried Dosage Forms, in Formulation and Process Development Strategies for Manufacturing Biopharmaceuticals (eds F. Jameel and S. Hershenson), John Wiley & Sons, Inc., Hoboken, NJ, USA
    • (2010) Formulation and Process Development Strategies for Manufacturing Biopharmaceuticals
    • Shalaev, E.Y.1    Gatlin, L.A.2
  • 18
    • 33645073012 scopus 로고    scopus 로고
    • Pain perception after subcutaneous injections of media containing different buffers
    • Laursen, T., Hansen, B., Fisker, S. (2006) Pain Perception After Subcutaneous Injections of Media Containing Different Buffers. Basic & Clinical Pharmacology & Toxicology. 98, 218-221
    • (2006) Basic & Clinical Pharmacology & Toxicology. , vol.98 , pp. 218-221
    • Laursen, T.1    Hansen, B.2    Fisker, S.3
  • 19
    • 0031962703 scopus 로고    scopus 로고
    • Pain at the injection site of subcutaneously administered erythropoietin: Phosphate-buffered epoetin alpha compared to citrate-buffered epoetin alpha and epoetin beta
    • Veys, N., Dhondt, A., Lameire, N., (1998) Pain at the Injection Site of Subcutaneously Administered Erythropoietin: Phosphate-Buffered Epoetin Alpha Compared to Citrate-Buffered Epoetin Alpha and Epoetin Beta. Clin. Nephrol. 49, 41-44
    • (1998) Clin. Nephrol. , vol.49 , pp. 41-44
    • Veys, N.1    Dhondt, A.2    Lameire, N.3
  • 20
    • 0031845014 scopus 로고    scopus 로고
    • Pain perception following subcutaneous injections of citrate-buffered and phosphate-buffered epoetin alpha
    • Yu, A. W., Leung, C. B., Li, P. K., Lui, S. F., Lai, K. N. (1998) Pain Perception Following Subcutaneous Injections of Citrate-Buffered and Phosphate-Buffered Epoetin Alpha. Int. J. Artif. Organs. 21, 341-343
    • (1998) Int. J. Artif. Organs. , vol.21 , pp. 341-343
    • Yu, A.W.1    Leung, C.B.2    Li, P.K.3    Lui, S.F.4    Lai, K.N.5
  • 21
    • 0035379916 scopus 로고    scopus 로고
    • Kinetic and thermodynamic analysis of thermal unfolding of recombinant erythropoietin
    • Arakawa, T., Philo, J.S., Kita, Y. (2001) Kinetic and Thermodynamic Analysis of Thermal Unfolding of Recombinant Erythropoietin. Biosci. Biotechnol. Biochem. 65, 1321-1327
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 1321-1327
    • Arakawa, T.1    Philo, J.S.2    Kita, Y.3
  • 22
    • 0037453298 scopus 로고    scopus 로고
    • Relationship between stability of folding intermediates and amyloid formation for the yeast prion ure2p: A quantitative analysis of the effects of ph and buffer system
    • Zhu, L, Zhang, XJ., Wang, L. Y., Zhou, J. M., Perrett, S. (2003) Relationship between Stability of Folding Intermediates and Amyloid Formation for the Yeast Prion Ure2p: A Quantitative Analysis of the Effects of pH and Buffer System. J. Mol. Biol. 328, 235-254
    • (2003) J. Mol. Biol. , vol.328 , pp. 235-254
    • Zhu, L.1    Zhang, X.J.2    Wang, L.Y.3    Zhou, J.M.4    Perrett, S.5
  • 23
    • 35448968555 scopus 로고    scopus 로고
    • Biotechnology applications of amino acids in protein purification and formulations
    • Arakawa, T. Tsumoto, K., Kita, Y., Chang, B., Ejima D. (2007) Biotechnology Applications of Amino Acids in Protein Purification and Formulations. Amino Acids. 33, 587-605
    • (2007) Amino Acids. , vol.33 , pp. 587-660
    • Arakawa Tsumoto, T.K.1    Kita, Y.2    Chang, B.3    Ejima, D.4
  • 24
    • 0346846691 scopus 로고    scopus 로고
    • Influence of histidine on the stability and physical properties of a fully human antibody in aqueous and solid forms
    • Chen, B., Bautista, R, Yu, K., Zapata, G. A., Mulkerrin, M. G., Chamow, S. M. (2003) Influence of Histidine on the Stability and Physical Properties of a Fully Human Antibody in Aqueous and Solid Forms. Pharmacol. Res. 20, 1952-1960
    • (2003) Pharmacol. Res. , vol.20 , pp. 1952-1960
    • Chen, B.1    Bautista, R.2    Yu, K.3    Zapata, G.A.4    Mulkerrin, M.G.5    Chamow, S.M.6
  • 25
    • 33947716232 scopus 로고    scopus 로고
    • Spectroscopic evaluation of the stabilization of humanized monoclonal antibodies in amino acid formulations
    • Tian, F., Middaugh, C. R, Offerdahl, T., Munsona, E., Sane, S., Rytting, J. H. (2007) Spectroscopic Evaluation of the Stabilization of Humanized Monoclonal Antibodies in Amino Acid Formulations. Int. J. Pharmaceutics. 335, 20-31
    • (2007) Int. J. Pharmaceutics. , vol.335 , pp. 20-31
    • Tian, F.1    Middaugh, C.R.2    Offerdahl, T.3    Munsona, E.4    Sane, S.5    Rytting, J.H.6
  • 27
    • 0032104360 scopus 로고    scopus 로고
    • Antioxidant characteristics of l-histidine
    • Wade, A. M., Tucker, H.N. (1998) Antioxidant Characteristics of L-Histidine. J. Nutr. Biochem. 9, 308-315
    • (1998) J. Nutr. Biochem. , vol.9 , pp. 308-315
    • Wade, A.M.1    Tucker, H.N.2
  • 29
    • 30744439811 scopus 로고    scopus 로고
    • Influence of ph, buffer species, and storage temperature on physicochemical stability of a humanized monoclonal antibody la298
    • Zheng, J. Y., Janis, L. J., (2006) Influence of pH, Buffer Species, and Storage Temperature on Physicochemical Stability of a Humanized Monoclonal Antibody LA298. Int. J. Pharmaceutics. 308, 46 51
    • (2006) Int. J. Pharmaceutics. , vol.308 , pp. 46-51
    • Zheng, J.Y.1    Janis, L.J.2
  • 30
    • 58849104102 scopus 로고    scopus 로고
    • Freeze-drying of proteins in glass solids formed by basic amino acids and dicarboxylic acids
    • Izutsu, K. I., Kadoya, S., Yomota, C, Kawanishi, T, Yonemochi, E., Terada, K. (2009) Freeze-Drying of Proteins in Glass Solids Formed by Basic Amino Acids and Dicarboxylic Acids. Chem. Pharm. Bull. 57, 43-48
    • (2009) Chem. Pharm. Bull. , vol.57 , pp. 43-48
    • Izutsu, K.I.1    Kadoya, S.2    Yomota, C.3    Kawanishi, T.4    Yonemochi, E.5    Terada, K.6
  • 31
  • 33
    • 3242798849 scopus 로고    scopus 로고
    • Simple method for improving protein solubility and long-term stability
    • GolovanovA.P., Hautbergue G.M., Wilson S.A., Lian L.Y. (2004) Simple Method for Improving Protein Solubility and Long-Term Stability. J. Am. Chem. Soc. 126, 8933-8939
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8933-9893
    • Golovanov, A.P.1    Hautbergue, G.M.2    Wilson, S.A.3    Lian, L.Y.4
  • 34
    • 0028895083 scopus 로고
    • A new strategy for enhancing the stability of lyophilized protein: The effect of the reconstitution medium on keratinocyte growth factor
    • Zhang M.Z., Wen J., Arakawa T., Prestrelski S.J. (1995) A New Strategy for Enhancing the Stability of Lyophilized Protein: The Effect of the Reconstitution Medium on Keratinocyte Growth Factor. Pharmacol. Res. 12, 1447-1452
    • (1995) Pharmacol. Res. , vol.12 , pp. 1447-1452
    • Zhang, M.Z.1    Wen, J.2    Arakawa, T.3    Prestrelski, S.J.4
  • 35
    • 0029986925 scopus 로고    scopus 로고
    • The effect of the reconstitution medium on aggregation of lyophilized recombinant lnterieukin-2 and ribonuclease a
    • Zhang M.Z., Pikal K., Nguyen T, Arakawa T, Prestrelski S.J. (1996) The Effect of the Reconstitution Medium on Aggregation of Lyophilized Recombinant lnterieukin-2 and Ribonuclease A. Pharmacol. Res. 13: 643-646
    • (1996) Pharmacol. Res. , vol.13 , pp. 643-646
    • Zhang, M.Z.1    Pikal, K.2    Nguyen, T.3    Arakawa, T.4    Prestrelski, S.J.5
  • 36
    • 0021067853 scopus 로고
    • Minimizing the aggregation of neutral insulin solutions
    • Quinn, R, Andrade, J. D. (1983) Minimizing the Aggregation of Neutral Insulin Solutions. J. Pharm. Sci. 72, 1472-1473
    • (1983) J. Pharm. Sci. , vol.72 , pp. 1472-1473
    • Quinn, R.1    Andrade, J.D.2
  • 37
    • 0019417691 scopus 로고
    • Prevention of insulin aggregation by dicarboxylic amino acids during prolonged infusion
    • Bringer, J., Heldt, A., Grodsky, G.M. (1981) Prevention of Insulin Aggregation by Dicarboxylic Amino Acids during Prolonged Infusion. Diabetes, 30, 83-85
    • (1981) Diabetes , vol.30 , pp. 83-88
    • Bringer, J.1    Heldt, A.2    Grodsky, G.M.3
  • 38
    • 0032967544 scopus 로고    scopus 로고
    • Inhibition of protein denaturation by fatty acids, bile salts and other natural substances: A new hypothesis for the mechanism of action of fish oil in rheumatic diseases
    • Saso, L., Valentini, G., Casini, M.L., Matti, E., Braghiroli, L., Mazzanti, G., Panzironi, C, Grippa, E., Silvestrini, B. (1999) Inhibition of Protein Denaturation by Fatty Acids, Bile Salts and Other Natural Substances: A New Hypothesis for the Mechanism of Action of Fish Oil in Rheumatic Diseases. Jpn. J. Pharmacol.79, 89-99
    • (1999) Jpn. J. Pharmacol. , vol.79 , pp. 89-99
    • Saso, L.1    Valentini, G.2    Casini, M.L.3    Matti, E.4    Braghiroli, L.5    Mazzanti, G.6    Panzironi, C.7    Grippa, E.8    Silvestrini, B.9
  • 40
    • 70350223665 scopus 로고    scopus 로고
    • Carboxylate-dependent gelation of a monoclonal antibody
    • Esue, O., Kanai, S., Liu, J., Patapoff, T. W. Shire, S. J., (2009) Carboxylate-Dependent Gelation of a Monoclonal Antibody. Pharm. Res. 26, 2478-2485
    • (2009) Pharm. Res. , vol.26 , pp. 2478-3248
    • Esue, O.1    Kanai, S.2    Liu, J.3    Patapoff, T.W.4    Shire, S.J.5
  • 41
    • 79951916297 scopus 로고    scopus 로고
    • Predicting the crystallization propensity of carboxylic acid buffers in frozen systems - Relevance to freeze- drying
    • Sundaramurthi, P., Suryanarayanan, R., (2011) Predicting the Crystallization Propensity of Carboxylic Acid Buffers in Frozen Systems - Relevance to Freeze- Drying. J. Pharm. Sci. 100, 1288-1293
    • (2011) J. Pharm. Sci. , vol.100 , pp. 1288-1293
    • Sundaramurthi, P.1    Suryanarayanan, R.2
  • 42
    • 79957597346 scopus 로고    scopus 로고
    • Thermophysical properties of carboxylic and amino acid buffers at subzero temperatures: Relevance to frozen state stabilization
    • Sundaramurthi, P., Suryanarayanan, R., (2011) Thermophysical Properties of Carboxylic and Amino Acid Buffers at Subzero Temperatures: Relevance to Frozen State Stabilization. J. Phys. Chem. B. 115, 7154-7164
    • (2011) J. Phys. Chem. B. , vol.115 , pp. 7154-7164
    • Sundaramurthi, P.1    Suryanarayanan, R.2


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