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Volumn 13, Issue 8, 1996, Pages 1142-1153

Solid-state stability of human insulin I. Mechanism and the effect of water on the kinetics of degradation in lyophiles from pH 2-5 solutions

Author keywords

Acyl transfer; Covalent dimerization; Deamidation; Intramolecular catalysis; Protein stability; Solid state degradation

Indexed keywords

HUMAN INSULIN; PENTEX; UNCLASSIFIED DRUG;

EID: 0029764145     PISSN: 07248741     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1016043715791     Document Type: Article
Times cited : (60)

References (47)
  • 2
    • 0026546241 scopus 로고
    • Pharmaceutics of protein drugs
    • R. Pearlman and T. H. Nguyen. Pharmaceutics of protein drugs. J. Pharm. Pharmacol. 44 (Suppl.): 178-185 (1992).
    • (1992) J. Pharm. Pharmacol. , vol.44 , Issue.SUPPL. , pp. 178-185
    • Pearlman, R.1    Nguyen, T.H.2
  • 3
    • 0003220389 scopus 로고
    • Freeze-drying of proteins: Process, formulation and stability
    • J. L. Cleland, R. Langer, (ed.) American Chemical Society, Washington, D.C.
    • M. J. Pikal. Freeze-drying of proteins: Process, formulation and stability. In J. L. Cleland, R. Langer, (ed.) Formulation and Delivery of Proteins and Peptides, American Chemical Society, Washington, D.C., 1994, 120-133.
    • (1994) Formulation and Delivery of Proteins and Peptides , pp. 120-133
    • Pikal, M.J.1
  • 4
    • 0003161362 scopus 로고
    • Parenteral formulations of proteins and peptides: Stability and stabilizers
    • Y. C. J. Wang and M. A. Hanson. Parenteral formulations of proteins and peptides: stability and stabilizers. J. Parenteral Sci. Techn. 42:S1-S24 (1988).
    • (1988) J. Parenteral Sci. Techn. , vol.42
    • Wang, Y.C.J.1    Hanson, M.A.2
  • 5
    • 0023803010 scopus 로고
    • The role of moisture in protein stability
    • M. J. Hageman. The role of moisture in protein stability. Drug Dev. Ind. Pharm. 14:2047-2070 (1988).
    • (1988) Drug Dev. Ind. Pharm. , vol.14 , pp. 2047-2070
    • Hageman, M.J.1
  • 7
    • 0026071674 scopus 로고
    • Moisture-induced aggregation of lyophilized proteins in the solid state
    • W. R. Liu, R. Langer and A. M. Klibanov. Moisture-induced aggregation of lyophilized proteins in the solid state. Biotech. Bioeng. 37:177-184 (1991).
    • (1991) Biotech. Bioeng. , vol.37 , pp. 177-184
    • Liu, W.R.1    Langer, R.2    Klibanov, A.M.3
  • 8
    • 0021994379 scopus 로고
    • Haemoglobin lyophilized with sucrose: The effect of residual moisture on storage
    • T. I. Pristoupil, M. Kramlova, H. Fortova and S. Ulrych. Haemoglobin lyophilized with sucrose: the effect of residual moisture on storage. Haematologia 18:45-52 (1985).
    • (1985) Haematologia , vol.18 , pp. 45-52
    • Pristoupil, T.I.1    Kramlova, M.2    Fortova, H.3    Ulrych, S.4
  • 9
    • 0026356940 scopus 로고
    • The effects of formulation and moisture on the stability of a freezedried monoclonal antibody-vinca conjugate: A test of the WLF glass transition theory
    • M. L. Roy, M. J. Pikal, E. C. Rickard and A. M. Maloney. The effects of formulation and moisture on the stability of a freezedried monoclonal antibody-vinca conjugate: A test of the WLF glass transition theory. Dev. Biol. Standard 74:323-340 (1992).
    • (1992) Dev. Biol. Standard , vol.74 , pp. 323-340
    • Roy, M.L.1    Pikal, M.J.2    Rickard, E.C.3    Maloney, A.M.4
  • 10
    • 0002493506 scopus 로고
    • Interpreting the behavior of low moisture foods
    • T. M. Hardman, (ed.) Elsevier Applied Science, London
    • H. Levine and L. Slade. Interpreting the behavior of low moisture foods. In T. M. Hardman, (ed.) Water and Food Quality, Elsevier Applied Science, London, 1989, 71-134.
    • (1989) Water and Food Quality , pp. 71-134
    • Levine, H.1    Slade, L.2
  • 11
    • 0003002854 scopus 로고
    • Protein-water interactions: Water as a plasticizer of gluten and other protein polymers
    • R. D. Phillips, J. W. Finley, (ed.) Dekker, New York
    • L. Slade, H. Levine and J. W. Finley. Protein-water interactions: Water as a plasticizer of gluten and other protein polymers. In R. D. Phillips, J. W. Finley, (ed.) Protein Quality and the Effects of Processing, Dekker, New York, 1989, 9-124.
    • (1989) Protein Quality and the Effects of Processing , pp. 9-124
    • Slade, L.1    Levine, H.2    Finley, J.W.3
  • 12
    • 0025399132 scopus 로고
    • Differential scanning calorimetry study of phase transitions affecting quality of dehydrated materials
    • Y. Roos and M. Karel. Differential scanning calorimetry study of phase transitions affecting quality of dehydrated materials. Biotechnol. Prog. 6:159-163 (1990).
    • (1990) Biotechnol. Prog. , vol.6 , pp. 159-163
    • Roos, Y.1    Karel, M.2
  • 13
    • 0002005744 scopus 로고
    • X-ray diffractometer and microscopic investigation of crystallization of amorphous sucrose
    • K. J. Palmer, W. B. Dye and D. Black. X-ray diffractometer and microscopic investigation of crystallization of amorphous sucrose. J. Agric. Food Chem. 4:77-81 (1956).
    • (1956) J. Agric. Food Chem. , vol.4 , pp. 77-81
    • Palmer, K.J.1    Dye, W.B.2    Black, D.3
  • 14
    • 0020611893 scopus 로고
    • Hygroscopicity and solubility of noncrystalline cephalexin
    • M. Otsuka and N. Kaneniwa. Hygroscopicity and solubility of noncrystalline cephalexin. Chem. Pharm. Bull. 31:230-236 (1983).
    • (1983) Chem. Pharm. Bull. , vol.31 , pp. 230-236
    • Otsuka, M.1    Kaneniwa, N.2
  • 15
    • 33947462374 scopus 로고
    • Equilibrium moisture content and crystallization of amorphous sucrose and glucose
    • B. Makower and W. B. Dye. Equilibrium moisture content and crystallization of amorphous sucrose and glucose. J. Agric. Food Chem. 4:72-77 (1956).
    • (1956) J. Agric. Food Chem. , vol.4 , pp. 72-77
    • Makower, B.1    Dye, W.B.2
  • 16
    • 0024404092 scopus 로고
    • Glassy state of pharmaceuticals. III. Thermal properties and stability of glassy pharmaceuticals and their binary glass systems
    • E. Fukuoka, M. Makita and S. Yamamura. Glassy state of pharmaceuticals. III. Thermal properties and stability of glassy pharmaceuticals and their binary glass systems. Chem. Pharm. Bull. 37:1047-1050 (1989).
    • (1989) Chem. Pharm. Bull. , vol.37 , pp. 1047-1050
    • Fukuoka, E.1    Makita, M.2    Yamamura, S.3
  • 18
    • 0017647381 scopus 로고
    • Thermal decomposition of amorphous β-lactam antibiotics
    • M. J. Pikal, A. L. Lukes and J. E. Lang. Thermal decomposition of amorphous β-lactam antibiotics. J. Pharm. Sci. 66:1312-1316 (1977).
    • (1977) J. Pharm. Sci. , vol.66 , pp. 1312-1316
    • Pikal, M.J.1    Lukes, A.L.2    Lang, J.E.3
  • 19
    • 0029015405 scopus 로고
    • Molecular mobility of amorphous pharmaceutical solids below their glass transition temperatures
    • B. C. Hancock, S. L. Shamblin and G. Zografi. Molecular mobility of amorphous pharmaceutical solids below their glass transition temperatures. Pharm. Res. 12:799-806 (1995).
    • (1995) Pharm. Res. , vol.12 , pp. 799-806
    • Hancock, B.C.1    Shamblin, S.L.2    Zografi, G.3
  • 20
    • 0000652983 scopus 로고
    • Preformulation studies oriented toward sustained delivery of recombinant somatotropins
    • M. J. Hageman, J. M. Bauer, P. L. Possert and R. T. Darrington. Preformulation studies oriented toward sustained delivery of recombinant somatotropins. J. Agric. Food Chem. 40:348-355 (1992).
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 348-355
    • Hageman, M.J.1    Bauer, J.M.2    Possert, P.L.3    Darrington, R.T.4
  • 21
    • 0009372381 scopus 로고
    • Solution and solid state chemical instabilities of asparaginyl and aspartyl residues in model peptides
    • J. L. Cleland, R. Langer, (ed.) American Chemical Society, Washington, D.C.
    • C. Oliyai and R. T. Borchardt. Solution and solid state chemical instabilities of asparaginyl and aspartyl residues in model peptides. In J. L. Cleland, R. Langer, (ed.) Formulation and Delivery of Proteins and Peptides, American Chemical Society, Washington, D.C., 1994, 46-58.
    • (1994) Formulation and Delivery of Proteins and Peptides , pp. 46-58
    • Oliyai, C.1    Borchardt, R.T.2
  • 22
    • 0028301459 scopus 로고
    • The role of intramolecular nucleophilic catalysis and the effects of self-association on the deamidation of human insulin at low pH
    • R. T. Darrington and B. D. Anderson. The role of intramolecular nucleophilic catalysis and the effects of self-association on the deamidation of human insulin at low pH. Pharm. Res. 11:784-793 (1994).
    • (1994) Pharm. Res. , vol.11 , pp. 784-793
    • Darrington, R.T.1    Anderson, B.D.2
  • 23
    • 0028998979 scopus 로고
    • Effects of insulin concentration and self-association of its A-21 cyclic anhydride intermediate to desamido insulin and covalent dimer
    • R. T. Darrington and B. D. Anderson. Effects of insulin concentration and self-association of its A-21 cyclic anhydride intermediate to desamido insulin and covalent dimer. Pharm. Res. 12:1077-1084 (1995).
    • (1995) Pharm. Res. , vol.12 , pp. 1077-1084
    • Darrington, R.T.1    Anderson, B.D.2
  • 24
    • 0028931574 scopus 로고
    • Evidence for a common intermediate in insulin deamidation and covalent dimer formation: Effects of pH and aniline trapping in dilute acidic solutions
    • R. T. Darrington and B. D. Anderson. Evidence for a common intermediate in insulin deamidation and covalent dimer formation: Effects of pH and aniline trapping in dilute acidic solutions. J. Pharm. Sci. 84:275-282 (1995).
    • (1995) J. Pharm. Sci. , vol.84 , pp. 275-282
    • Darrington, R.T.1    Anderson, B.D.2
  • 25
    • 12444272525 scopus 로고
    • Adsorption of gases in multimolecular layers
    • S. Brunauer, P. H. Emmett and E. Teller. Adsorption of gases in multimolecular layers. J. Am. Chem. Soc. 60:309-319 (1938).
    • (1938) J. Am. Chem. Soc. , vol.60 , pp. 309-319
    • Brunauer, S.1    Emmett, P.H.2    Teller, E.3
  • 26
    • 0002206625 scopus 로고
    • Water activity and its estimation in food systems: Theoretical aspects
    • L. B. Rockland, G. F. Stewart, (ed.) Academic Press, New York
    • C. van den Berg and S. Bruin. Water activity and its estimation in food systems: Theoretical aspects. In L. B. Rockland, G. F. Stewart, (ed.) Water Activity: Influences of Food Quality, Academic Press, New York, 1981, 1-61.
    • (1981) Water Activity: Influences of Food Quality , pp. 1-61
    • Van Den Berg, C.1    Bruin, S.2
  • 27
    • 0022389697 scopus 로고
    • Fingerprint analysis of insulin and proinsulins
    • U. Grau. Fingerprint analysis of insulin and proinsulins. Diabetes 34:1174-1180 (1985).
    • (1985) Diabetes , vol.34 , pp. 1174-1180
    • Grau, U.1
  • 28
    • 0019320989 scopus 로고
    • Correlation of IR spectroscopic, heat capacity, diamagnetic susceptibility and enzymatic measurements on lysozyme powder
    • G. Careri, E. Gratton, P.-H. Yang and J. A. Rupley. Correlation of IR spectroscopic, heat capacity, diamagnetic susceptibility and enzymatic measurements on lysozyme powder. Nature 284:572-573 (1980).
    • (1980) Nature , vol.284 , pp. 572-573
    • Careri, G.1    Gratton, E.2    Yang, P.-H.3    Rupley, J.A.4
  • 29
    • 0021485335 scopus 로고
    • Sequential hydration of dry proteins: A direct difference IR investigation of sequence homologs lysozyme and α-lactalbumin
    • P. L. Poole and J. L. Finney. Sequential hydration of dry proteins: A direct difference IR investigation of sequence homologs lysozyme and α-lactalbumin. Biopolymers 23:1647-1666 (1984).
    • (1984) Biopolymers , vol.23 , pp. 1647-1666
    • Poole, P.L.1    Finney, J.L.2
  • 30
    • 0025039869 scopus 로고
    • The relationship between the glass transition temperature and water vapor absorption by poly(vinylpyrrolidone)
    • C. A. Oksanen and G. Zografi. The relationship between the glass transition temperature and water vapor absorption by poly(vinylpyrrolidone). Pharm. Res. 7:654-657 (1990).
    • (1990) Pharm. Res. , vol.7 , pp. 654-657
    • Oksanen, C.A.1    Zografi, G.2
  • 31
    • 0027174285 scopus 로고
    • Molecular mobility in mixtures of absorbed water and solid poly(vinylpyrrolidone)
    • C. A. Oksanen and G. Zografi. Molecular mobility in mixtures of absorbed water and solid poly(vinylpyrrolidone). Pharm. Res. 10:791-799 (1993).
    • (1993) Pharm. Res. , vol.10 , pp. 791-799
    • Oksanen, C.A.1    Zografi, G.2
  • 32
    • 0002459877 scopus 로고
    • Water as a plasticizer: Physico-chemical aspects of low-moisture polymeric systems
    • F. Franks, (ed.) Cambridge University Press, Cambridge
    • H. Levine and L. Slade. Water as a plasticizer: Physico-chemical aspects of low-moisture polymeric systems. In F. Franks, (ed.) Water Science Reviews, Cambridge University Press, Cambridge, 1987, 79-185.
    • (1987) Water Science Reviews , pp. 79-185
    • Levine, H.1    Slade, L.2
  • 33
    • 0025102704 scopus 로고
    • The molecular basis of moisture effects on the physical and chemical stability of drugs in the solid state
    • C. Ahlneck and G. Zografi. The molecular basis of moisture effects on the physical and chemical stability of drugs in the solid state. Int. J. Pharm. 62:87-95 (1990).
    • (1990) Int. J. Pharm. , vol.62 , pp. 87-95
    • Ahlneck, C.1    Zografi, G.2
  • 34
    • 0027941825 scopus 로고
    • Structural details of Asp(B9) human insulin at low pH from two-dimensional NMR titration studies
    • M. D. Sorenson and J. J. Led. Structural details of Asp(B9) human insulin at low pH from two-dimensional NMR titration studies. Biochemistry 33:13727-13733 (1994).
    • (1994) Biochemistry , vol.33 , pp. 13727-13733
    • Sorenson, M.D.1    Led, J.J.2
  • 36
    • 0019473990 scopus 로고
    • Chemical properties of the functional groups of insulin
    • Y.-K. Chan, G. Oda and H. Kaplan. Chemical properties of the functional groups of insulin. Biochem. J. 193:419-425 (1981).
    • (1981) Biochem. J. , vol.193 , pp. 419-425
    • Chan, Y.-K.1    Oda, G.2    Kaplan, H.3
  • 37
    • 0025793265 scopus 로고
    • The effects of formulation variables on the stability of freeze-dried human growth hormone
    • M. J. Pikal, K. M. Dellerman, M. L. Roy and R. M. Riggin. The effects of formulation variables on the stability of freeze-dried human growth hormone. Pharm. Res. 8:427-436 (1991).
    • (1991) Pharm. Res. , vol.8 , pp. 427-436
    • Pikal, M.J.1    Dellerman, K.M.2    Roy, M.L.3    Riggin, R.M.4
  • 38
    • 0027137331 scopus 로고
    • Thermal deamidation of proteins in a restricted water environment
    • J. Zhang, T. C. Lee and C.-T. Ho. Thermal deamidation of proteins in a restricted water environment. J. Agric. Food Chem. 41:1840-1843 (1993).
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 1840-1843
    • Zhang, J.1    Lee, T.C.2    Ho, C.-T.3
  • 39
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides: Succinimide-linked reactions that contribute to protein degradation
    • T. Geiger and S. Clarke. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides: Succinimide-linked reactions that contribute to protein degradation. J. Biol. Chem. 262:785-794 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 40
    • 0025121123 scopus 로고
    • High-performance liquid chromatography (HPLC) and HPLC-mass spectroscopic (MS) analysis of the degradation of the luteinizing hormone-releasing hormone (LH-RH) antagonist RS-26306 in aqueous solution
    • R. G. Strickley, M. Brandi, K. W. Chan, K. Straug and L. Gu. High-performance liquid chromatography (HPLC) and HPLC-mass spectroscopic (MS) analysis of the degradation of the luteinizing hormone-releasing hormone (LH-RH) antagonist RS-26306 in aqueous solution. Pharm. Res. 7:530-536 (1990).
    • (1990) Pharm. Res. , vol.7 , pp. 530-536
    • Strickley, R.G.1    Brandi, M.2    Chan, K.W.3    Straug, K.4    Gu, L.5
  • 41
    • 0028343435 scopus 로고
    • Chemical pathways of peptide degradation. VII. Solid state chemical instability of an aspartyl residue in a model hexapeptide
    • C. Oliyai, J. P. Patel, L. Carr and R. T. Borchardt. Chemical pathways of peptide degradation. VII. Solid state chemical instability of an aspartyl residue in a model hexapeptide. Pharm. Res. 11:901-908 (1994).
    • (1994) Pharm. Res. , vol.11 , pp. 901-908
    • Oliyai, C.1    Patel, J.P.2    Carr, L.3    Borchardt, R.T.4
  • 42
    • 0028234747 scopus 로고
    • Major degradation products of basic fibroblast growth factor: Detection of succinimide and iso-aspartate in place of aspartate
    • Z. Shahrokh, G. Eberlein, D. Buckley, M. V. Paranandi, D. W. Aswad, P. Stratton, R. Mischak and Y. J. Wang. Major degradation products of basic fibroblast growth factor: Detection of succinimide and iso-aspartate in place of aspartate. Pharm. Res. 11:936-944 (1994).
    • (1994) Pharm. Res. , vol.11 , pp. 936-944
    • Shahrokh, Z.1    Eberlein, G.2    Buckley, D.3    Paranandi, M.V.4    Aswad, D.W.5    Stratton, P.6    Mischak, R.7    Wang, Y.J.8
  • 43
    • 0028897492 scopus 로고
    • Chemical pathways of degradation of the bradykinin analog, RMP-7
    • J. A. Straub, A. Akiyama, P. Parmar and G. F. Musso. Chemical pathways of degradation of the bradykinin analog, RMP-7. Pharm. Res. 12:305-308 (1995).
    • (1995) Pharm. Res. , vol.12 , pp. 305-308
    • Straub, J.A.1    Akiyama, A.2    Parmar, P.3    Musso, G.F.4
  • 44
    • 0009071257 scopus 로고
    • Formation of glasses from liquids and biopolymers
    • C. A. Angell. Formation of glasses from liquids and biopolymers. Science 267:1924-1935 (1995).
    • (1995) Science , vol.267 , pp. 1924-1935
    • Angell, C.A.1
  • 45
    • 0002398428 scopus 로고
    • Material science and the production of shelf-stable biologicals
    • F. Franks, R. H. M. Hatley and S. F. Mathias. Material science and the production of shelf-stable biologicals. Biopharm. 4:38-55 (1991).
    • (1991) Biopharm. , vol.4 , pp. 38-55
    • Franks, F.1    Hatley, R.H.M.2    Mathias, S.F.3
  • 46
    • 0026068176 scopus 로고
    • Beyond water activity: Recent advances based on an alternative approach to the assessment of food quality and safety
    • L. Slade and H. Levine. Beyond water activity: Recent advances based on an alternative approach to the assessment of food quality and safety. Crit. Rev. Food Sci. and Nutrit. 30:115-360 (1991).
    • (1991) Crit. Rev. Food Sci. and Nutrit. , vol.30 , pp. 115-360
    • Slade, L.1    Levine, H.2
  • 47
    • 0006343354 scopus 로고
    • Deuteron NMR relaxation studies of combined main-chain/side-chain polymers in the liquid crystalline and glassy state
    • K. Kohlhammer, G. Kothe, B. Reck and H. Ringsdorf. Deuteron NMR relaxation studies of combined main-chain/side-chain polymers in the liquid crystalline and glassy state. Ber. Bunsen-Ges. Phys. Chem. 93:1323-1325 (1989).
    • (1989) Ber. Bunsen-Ges. Phys. Chem. , vol.93 , pp. 1323-1325
    • Kohlhammer, K.1    Kothe, G.2    Reck, B.3    Ringsdorf, H.4


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