메뉴 건너뛰기




Volumn 94, Issue 2, 2005, Pages 382-396

Effects of benzyl alcohol on aggregation of recombinant human interleukin-1-receptor antagonist in reconstituted lyophilized formulations

Author keywords

Aggregation; Benzyl alcohol; rhIL 1ra

Indexed keywords

BENZYL ALCOHOL; PRESERVATIVE; RECOMBINANT INTERLEUKIN 1 RECEPTOR BLOCKING AGENT; SODIUM CHLORIDE; SUCROSE; WATER;

EID: 14344261247     PISSN: 00223549     EISSN: None     Source Type: Journal    
DOI: 10.1002/jps.20258     Document Type: Article
Times cited : (30)

References (45)
  • 1
    • 33645456486 scopus 로고    scopus 로고
    • Practical approaches to protein formulation development
    • Carpenter JF, Manning MC, editors. New York: Kluwer Academic
    • Chang BS, Hershenson S. 2002. Practical approaches to protein formulation development. In: Carpenter JF, Manning MC, editors. Rational design of stable protein formulation. New York: Kluwer Academic.
    • (2002) Rational Design of Stable Protein Formulation
    • Chang, B.S.1    Hershenson, S.2
  • 2
    • 0025870619 scopus 로고
    • Patient acceptance of Nordiject: A new drug delivery system for growth hormone
    • Jorgensen JT, Mortensen HB, Jorgensen JO. 1991. Patient acceptance of Nordiject: A new drug delivery system for growth hormone. DICP Ann Pharamacother 25:585-588.
    • (1991) DICP Ann Pharamacother , vol.25 , pp. 585-588
    • Jorgensen, J.T.1    Mortensen, H.B.2    Jorgensen, J.O.3
  • 3
    • 0021630221 scopus 로고
    • Considerations in selecting antimicrobial agents for parenteral product development
    • Akers MJ. 1984. Considerations in selecting antimicrobial agents for parenteral product development. Pharm Technol 8:36-46.
    • (1984) Pharm Technol , vol.8 , pp. 36-46
    • Akers, M.J.1
  • 4
    • 85030809707 scopus 로고    scopus 로고
    • Antimicrobial preservatives in sterile products: Issues and challenges with protein products
    • San Diego, CA
    • Akers MJ. 2001. Antimicrobial preservatives in sterile products: Issues and challenges with protein products. Proceedings of 2001 IBC Conference on Protein Formulation, San Diego, CA.
    • (2001) Proceedings of 2001 IBC Conference on Protein Formulation
    • Akers, M.J.1
  • 5
    • 0036828056 scopus 로고    scopus 로고
    • Excipient-drug interactions in parenteral formulations
    • Akers MJ. 2002. Excipient-drug interactions in parenteral formulations. J Pharm Sci 91:2283-2300.
    • (2002) J Pharm Sci , vol.91 , pp. 2283-2300
    • Akers, M.J.1
  • 7
    • 0030606850 scopus 로고    scopus 로고
    • Aggregation of recombinant human growth hormone induced by phenolic compounds
    • Maa YF, Hsu CC. 1996. Aggregation of recombinant human growth hormone induced by phenolic compounds. Int J Pharm 140:155-168.
    • (1996) Int J Pharm , vol.140 , pp. 155-168
    • Maa, Y.F.1    Hsu, C.C.2
  • 8
    • 0030947271 scopus 로고    scopus 로고
    • Solvent effects on the solubility and physical stability of insulin-like growth factor-I
    • Fransson J, Hallen D, Florin-Robertsson FE. 1997. Solvent effects on the solubility and physical stability of insulin-like growth factor-I. Pharm Res 14: 606-612.
    • (1997) Pharm Res , vol.14 , pp. 606-612
    • Fransson, J.1    Hallen, D.2    Florin-Robertsson, F.E.3
  • 9
    • 0030990078 scopus 로고    scopus 로고
    • The effect of benzyl alcohol on recombinant intereferon-gamma
    • Lam XM, Patapoff TW, Nguyen TH. 1997. The effect of benzyl alcohol on recombinant intereferon-gamma. Pharm Res 14:725-729.
    • (1997) Pharm Res , vol.14 , pp. 725-729
    • Lam, X.M.1    Patapoff, T.W.2    Nguyen, T.H.3
  • 10
    • 14444277713 scopus 로고    scopus 로고
    • Interleukin-1-receptor (IL-1R) liquid formulation development using differential scanning calorimetry
    • Remmele RL, Nightlinger NS, Srinivasan S, Gombotz WR. 1998. Interleukin-1-receptor (IL-1R) liquid formulation development using differential scanning calorimetry. Pharm Res 15:200-208.
    • (1998) Pharm Res , vol.15 , pp. 200-208
    • Remmele, R.L.1    Nightlinger, N.S.2    Srinivasan, S.3    Gombotz, W.R.4
  • 12
    • 0018974918 scopus 로고
    • Role of aggregated human growth hormone (Hgh) in development of antibodies to Hgh
    • Moore WV, Leppert P. 1980. Role of aggregated human growth hormone (Hgh) in development of antibodies to Hgh. J Clin Endocrinol Metab 51: 691-697.
    • (1980) J Clin Endocrinol Metab , vol.51 , pp. 691-697
    • Moore, W.V.1    Leppert, P.2
  • 13
    • 0025286235 scopus 로고
    • Persistent cutaneous insulin allergy resulting from high molecular weight insulin aggregates
    • Ratner RE, Phillips TM, Steiner M. 1990. Persistent cutaneous insulin allergy resulting from high molecular weight insulin aggregates. Diabetes 39: 728-733.
    • (1990) Diabetes , vol.39 , pp. 728-733
    • Ratner, R.E.1    Phillips, T.M.2    Steiner, M.3
  • 14
    • 0027475961 scopus 로고
    • Safety of intravenous imuunoglobulin
    • Thornton CA, Ballow M. 1993. Safety of intravenous imuunoglobulin. Arch Neurol 50:135-136.
    • (1993) Arch Neurol , vol.50 , pp. 135-136
    • Thornton, C.A.1    Ballow, M.2
  • 16
    • 84889404748 scopus 로고    scopus 로고
    • 58th ed. Oradell, NJ: Medical Economics
    • Physician's desk reference. 2004. 58th ed. Oradell, NJ: Medical Economics.
    • (2004) Physician's Desk Reference
  • 17
    • 0030443567 scopus 로고    scopus 로고
    • Surface induced denaturation of proteins during freezing and its inhibition by surfactants
    • Chang BS, Kendrick BS, Carpenter JF. 1996. Surface induced denaturation of proteins during freezing and its inhibition by surfactants. J Pharm Sci 85:1325-1330.
    • (1996) J Pharm Sci , vol.85 , pp. 1325-1330
    • Chang, B.S.1    Kendrick, B.S.2    Carpenter, J.F.3
  • 18
  • 19
    • 0036167323 scopus 로고    scopus 로고
    • A new mechanism for decreasing aggregation of recombinant human interferon-γ by a surfactant: Slowed dissolution of lyophilized formulations in a solution containing 0.03% polysorbate 20
    • Webb SD, Cleland JL, Carpenter JF, Randolph TW. 2001. A new mechanism for decreasing aggregation of recombinant human interferon-γ by a surfactant: Slowed dissolution of lyophilized formulations in a solution containing 0.03% polysorbate 20. J Pharm Sci 91:543-558.
    • (2001) J Pharm Sci , vol.91 , pp. 543-558
    • Webb, S.D.1    Cleland, J.L.2    Carpenter, J.F.3    Randolph, T.W.4
  • 20
    • 0029986925 scopus 로고    scopus 로고
    • The effect of reconstitution medium on aggregation of lyophilized recombinant interlukin-2 and ribonuclease a
    • Zhang MZ, Pikal K, Nguyen T, Arakawa T, Prestrelski SJ. 1996. The effect of reconstitution medium on aggregation of lyophilized recombinant interlukin-2 and ribonuclease A. J Pharm Sci 13: 643-646.
    • (1996) J Pharm Sci , vol.13 , pp. 643-646
    • Zhang, M.Z.1    Pikal, K.2    Nguyen, T.3    Arakawa, T.4    Prestrelski, S.J.5
  • 21
    • 0028895083 scopus 로고
    • A new strategy for enhancing the stability of lyophilized protein: The effect of reconstitution medium on keratinocyte growth factor
    • Zhang MZ, Wen J, Arakawa T, Prestrelski SJ. 1995. A new strategy for enhancing the stability of lyophilized protein: The effect of reconstitution medium on keratinocyte growth factor. Pharm Res 12:1447-1452.
    • (1995) Pharm Res , vol.12 , pp. 1447-1452
    • Zhang, M.Z.1    Wen, J.2    Arakawa, T.3    Prestrelski, S.J.4
  • 22
    • 0030044405 scopus 로고    scopus 로고
    • Development of a stable freeze dried formulation of recombinant human interleukin-1-receptor antagonist
    • Chang BS, Reeder G, Carpenter JF. 1996. Development of a stable freeze dried formulation of recombinant human interleukin-1-receptor antagonist. Pharm Res 13:242-249.
    • (1996) Pharm Res , vol.13 , pp. 242-249
    • Chang, B.S.1    Reeder, G.2    Carpenter, J.F.3
  • 23
    • 0030586287 scopus 로고    scopus 로고
    • Physical factors affecting the storage stability of freeze-dried interlukin-1 receptor antagonist: Glass transition and Conformation
    • Chang BS, Beauvais RM, Dong A, Carpenter JF. 1996c. Physical factors affecting the storage stability of freeze-dried interlukin-1 receptor antagonist: Glass transition and 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
  • 24
    • 0020322464 scopus 로고
    • Determination of residual moisture in freeze-dried viral vaccines: Karl Fisher, gravimetric and thermogravimetric methodologies
    • May JC, Grim E, Wheeler RM, West J. 1982. Determination of residual moisture in freeze-dried viral vaccines: Karl Fisher, gravimetric and thermogravimetric methodologies. J Biol Stand 10: 249-259.
    • (1982) J Biol Stand , vol.10 , pp. 249-259
    • May, J.C.1    Grim, E.2    Wheeler, R.M.3    West, J.4
  • 25
    • 0842289320 scopus 로고    scopus 로고
    • Effects of potassium bromide disk formation on the infrared spectra of dried model proteins
    • Meyer JD, Manning MC, Carpenter JF. 2004. Effects of potassium bromide disk formation on the infrared spectra of dried model proteins. J Pharm Sci 93:496-506.
    • (2004) J Pharm Sci , vol.93 , pp. 496-506
    • Meyer, J.D.1    Manning, M.C.2    Carpenter, J.F.3
  • 26
    • 0027163348 scopus 로고
    • Dehydration induced conformational transitions in proteins and their inhibition by stabilizers
    • Prestrelski SJ, Tedeschi N, Arakawa T, Carpenter JF. 1993. Dehydration induced conformational transitions in proteins and their inhibition by stabilizers. Biophys J 65:661-671.
    • (1993) Biophys J , vol.65 , pp. 661-671
    • Prestrelski, S.J.1    Tedeschi, N.2    Arakawa, T.3    Carpenter, J.F.4
  • 27
    • 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
  • 28
    • 0030059491 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
    • Kendrick BS, Dong A, Allison SD, Manning MC, Carpenter JF. 1995. 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.
    • (1995) 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
  • 29
    • 0030586740 scopus 로고    scopus 로고
    • Polymers protect lactate dehydrogenase during freeze-drying by inhibiting dissociation in the frozen state
    • Anchordoquy TJ, Carpenter JF. 1996. Polymers protect lactate dehydrogenase during freeze-drying by inhibiting dissociation in the frozen state. Arch Biochem Biophys 332:231.
    • (1996) Arch Biochem Biophys , vol.332 , pp. 231
    • Anchordoquy, T.J.1    Carpenter, J.F.2
  • 31
    • 0026691065 scopus 로고
    • Secondary structure and topology of interleukin-1-receptor antagonist protein determined by heteronuclear three dimensional NMR spectroscopy
    • Stockman BJ, Schaill TA, Roy M, Ulrich EL, Strakalaitis NA, Brunner DP, Yem WA, Deibel MR. 1992. Secondary structure and topology of interleukin-1-receptor antagonist protein determined by heteronuclear three dimensional NMR spectroscopy. Biochemistry 31:5237-5245.
    • (1992) Biochemistry , vol.31 , pp. 5237-5245
    • Stockman, B.J.1    Schaill, T.A.2    Roy, M.3    Ulrich, E.L.4    Strakalaitis, N.A.5    Brunner, D.P.6    Yem, W.A.7    Deibel, M.R.8
  • 32
    • 0030725266 scopus 로고    scopus 로고
    • Preferential exclusion of sucrose from recombinant human interlukin-1-receptor antagonist: Role is restricted conformational mobility and compaction of native state
    • Kendrick BS, Chang BS, Arakawa T, Peterson B, Randolph TW, Manning MC, Carpenter JF. 1997. Preferential exclusion of sucrose from recombinant human interlukin-1-receptor antagonist: Role is restricted conformational mobility and compaction of native state. Proc Natl Acad Sci USA 22:11917-11922.
    • (1997) Proc Natl Acad Sci USA , vol.22 , pp. 11917-11922
    • Kendrick, B.S.1    Chang, B.S.2    Arakawa, T.3    Peterson, B.4    Randolph, T.W.5    Manning, M.C.6    Carpenter, J.F.7
  • 33
    • 0000740448 scopus 로고
    • 4 on pH and composition during freezing
    • 4 on pH and composition during freezing. Arch Biochem Biophys 84:305-315.
    • (1959) Arch Biochem Biophys , vol.84 , pp. 305-315
    • Van Den Berg, L.1
  • 35
    • 14344255694 scopus 로고    scopus 로고
    • Freezing and drying induced structural changes in proteins and their inhibition by stabilizing additives
    • Ley R, May JC, editors. New York: Marcel Dekker
    • Carpenter JF, Izutsu K, Randolph TW. 1999. Freezing and drying induced structural changes in proteins and their inhibition by stabilizing additives. In: Ley R, May JC, editors. Pharmaceutical freeze drying. New York: Marcel Dekker.
    • (1999) Pharmaceutical Freeze Drying
    • Carpenter, J.F.1    Izutsu, K.2    Randolph, T.W.3
  • 36
    • 0031773791 scopus 로고    scopus 로고
    • Effects of tween 20 on agitation and freeze thawing induced aggregation of recombinant factor XIII
    • Krielgaard L, Jones L, Flink JM, Randolph TW, Carpenter JF. 1998. Effects of tween 20 on agitation and freeze thawing induced aggregation of recombinant factor XIII. J Pharm Sci 87: 1597.
    • (1998) J Pharm Sci , vol.87 , pp. 1597
    • Krielgaard, L.1    Jones, L.2    Flink, J.M.3    Randolph, T.W.4    Carpenter, J.F.5
  • 37
    • 0031660957 scopus 로고    scopus 로고
    • Effects of tween 80 and sucrose on acute short-term stability and long term storage at -20 degrees C of a recombinant hemoglobin
    • Kerwin BA, Heller MC, Levin SH, Randolph TW. 1998. Effects of tween 80 and sucrose on acute short-term stability and long term storage at -20 degrees C of a recombinant hemoglobin. J Pharm Sci 87:1062.
    • (1998) J Pharm Sci , vol.87 , pp. 1062
    • Kerwin, B.A.1    Heller, M.C.2    Levin, S.H.3    Randolph, T.W.4
  • 38
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solutions: Mechanism and driving forces in non native protein aggregation
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF. 2003. Physical stability of proteins in aqueous solutions: Mechanism and driving forces in non native protein aggregation. Pharm Res 20:1325-1336.
    • (2003) Pharm Res , vol.20 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 40
    • 0023905575 scopus 로고
    • The mechanism of cryoprotection of proteins by solutes
    • Carpenter JF, Crowe JH. 1988. The mechanism of cryoprotection of proteins by solutes. Cryobiology 25:244.
    • (1988) Cryobiology , vol.25 , pp. 244
    • Carpenter, J.F.1    Crowe, J.H.2
  • 41
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff SN. 1998. Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated. Adv Protein Chem 51:355.
    • (1998) Adv Protein Chem , vol.51 , pp. 355
    • Timasheff, S.N.1
  • 42
    • 0033562141 scopus 로고    scopus 로고
    • Hydrogen bonding between sugar and protein is responsible for inhibiting dehydration-induced protein unfolding
    • Allison SD, Randolph TW, Chang BS, Carpenter JF. 1999. Hydrogen bonding between sugar and protein is responsible for inhibiting dehydration-induced protein unfolding. Arch Biochem Biophys 365:289.
    • (1999) Arch Biochem Biophys , vol.365 , pp. 289
    • Allison, S.D.1    Randolph, T.W.2    Chang, B.S.3    Carpenter, J.F.4
  • 43
    • 0030043206 scopus 로고    scopus 로고
    • Proteins in frozen solutions: Evidence of ice-induced partial unfolding
    • Strambini GB, Gabellieri E. 1996. Proteins in frozen solutions: Evidence of ice-induced partial unfolding. Biophys J 70:971-976.
    • (1996) Biophys J , vol.70 , pp. 971-976
    • Strambini, G.B.1    Gabellieri, E.2
  • 44
    • 0027272126 scopus 로고
    • Freeze-thaw studies of a model protein, lactate dehydogenase in the presence of cryoprotectants
    • Nema S, Avis KE. 1993. Freeze-thaw studies of a model protein, lactate dehydogenase in the presence of cryoprotectants. J Parent Sci Technol 47: 76-83.
    • (1993) J Parent Sci Technol , vol.47 , pp. 76-83
    • Nema, S.1    Avis, K.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.