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Volumn 28, Issue 7, 2011, Pages 1591-1605

High-throughput screening of excipients intended to prevent antigen aggregation at air-liquid interface

Author keywords

excipients; fluorescence spectroscopy; high throughput screening; protein aggregation; vaccines

Indexed keywords

2 HYDROXYPROPYL BETA CYCLODEXTRIN; AMINO ACID; ANTIGEN 18A; ARGININE; ASPARTIC ACID; CYCLODEXTRIN; DOCUSATE SODIUM; EXCIPIENT; GAMMA CYCLODEXTRIN; GLYCINE; HISTIDINE; ISOLEUCINE; LEUCINE; MACROGOL STEARATE; MANNITOL; POLOXAMER; POLYMER; POLYOL; POLYSORBATE 80; POVIDONE; PROLINE; RECOMBINANT ANTIGEN; SERINE; SORBITOL; SUCROSE; SUGAR; SURFACTANT; THREONINE; TRYPTOPHAN; UNCLASSIFIED DRUG; VALINE;

EID: 79959868514     PISSN: 07248741     EISSN: 1573904X     Source Type: Journal    
DOI: 10.1007/s11095-011-0393-x     Document Type: Article
Times cited : (24)

References (44)
  • 1
    • 45149128290 scopus 로고    scopus 로고
    • Current perspectives on stability of protein drug products during formulation, fill and finish operations
    • DOI 10.1021/bp070462h
    • N Rathore RS Rajan 2008 Current perspectives on stability of protein drug products during formulation, fill and finish operations Biotechnol Prog. 24 3 504 514 18484778 10.1021/bp070462h 1:CAS:528:DC%2BD1cXlvFaktrc%3D (Pubitemid 351832704)
    • (2008) Biotechnology Progress , vol.24 , Issue.3 , pp. 504-514
    • Rathore, N.1    Rajan, R.S.2
  • 2
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • DOI 10.1016/j.ijpharm.2004.11.014, PII S0378517304006908
    • W Wang 2005 Protein aggregation and its inhibition in biopharmaceutics Int J Pharm. 289 1-2 1 30 15652195 10.1016/j.ijpharm.2004.11.014 1:CAS:528:DC%2BD2MXisFKjsg%3D%3D (Pubitemid 40093537)
    • (2005) International Journal of Pharmaceutics , vol.289 , Issue.1-2 , pp. 1-30
    • Wang, W.1
  • 3
    • 3042761213 scopus 로고    scopus 로고
    • Structure-immunogenicity relationships of therapeutic proteins
    • DOI 10.1023/B:PHAM.0000029275.41323.a6
    • S Hermeling DJ Crommelin H Schellekens W Jiskoot 2004 Structure-immunogenicity relationships of therapeutic proteins Pharm Res. 21 6 897 903 15212151 10.1023/B:PHAM.0000029275.41323.a6 1:CAS:528: DC%2BD2cXktlykurY%3D (Pubitemid 38870136)
    • (2004) Pharmaceutical Research , vol.21 , Issue.6 , pp. 897-903
    • Hermeling, S.1    Crommelin, D.J.A.2    Schellekens, H.3    Jiskoot, W.4
  • 4
    • 0032848275 scopus 로고    scopus 로고
    • Methods for studying protein adsorption
    • DOI 10.1016/S0076-6879(99)09028-X
    • V Hlady J Buijs HP Jennissen 1999 Methods for studying protein adsorption Methods Enzymol. 309 402 429 10507038 10.1016/S0076-6879(99)09028-X 1:CAS:528:DC%2BD3cXksVKgtQ%3D%3D (Pubitemid 29446463)
    • (1999) Methods in Enzymology , vol.309 , pp. 402-429
    • Hlady, V.1    Buijs, J.2    Jennissen, H.P.3
  • 6
    • 0029093065 scopus 로고
    • Aggregation of insulin and its prevention by carbohydrate excipients
    • 7552234 1:CAS:528:DyaK2MXotFems70%3D
    • M Katakam AK Banga 1995 Aggregation of insulin and its prevention by carbohydrate excipients PDA J Pharm Sci Technol. 49 4 160 165 7552234 1:CAS:528:DyaK2MXotFems70%3D
    • (1995) PDA J Pharm Sci Technol. , vol.49 , Issue.4 , pp. 160-165
    • Katakam, M.1    Banga, A.K.2
  • 7
    • 0019417691 scopus 로고
    • Prevention of insulin aggregation by dicarboxylic amino acids during prolonged infusion
    • J Bringer A Heldt GM Grodsky 1981 Prevention of insulin aggregation by dicarboxylic amino acids during prolonged infusion Diabetes. 30 1 83 85 6112178 10.2337/diabetes.30.1.83 1:CAS:528:DyaL3MXhs1altb0%3D (Pubitemid 11022629)
    • (1981) Diabetes , vol.30 , Issue.1 , pp. 83-85
    • Bringer, J.1    Heldt, A.2    Grodsky, G.M.3
  • 8
    • 28144453887 scopus 로고    scopus 로고
    • Evaluation of statistical design/modeling for prediction of the effect of amino acids on agitation-induced aggregation of human growth hormone and human insulin
    • S Soenderkaer M van de Weert LL Hansen J Flink S Frokjaer 2005 Evaluation of statistical design/modeling for prediction of the effect of amino acids on agitation-induced aggregation of human growth hormone and human insulin Drug Del Sci Tech. 15 427 434 1:CAS:528:DC%2BD28XktVyhsw%3D%3D (Pubitemid 41695890)
    • (2005) Journal of Drug Delivery Science and Technology , vol.15 , Issue.6 , pp. 427-434
    • Soenderkaer, S.1    Van De Weert, M.2    Lindgaard Hansen, L.3    Flink, J.4    Frokjaer, S.5
  • 9
    • 0021067853 scopus 로고
    • Minimizing the aggregation of neutral insulin solutions
    • R Quinn JD Andrade 1983 Minimizing the aggregation of neutral insulin solutions J Pharm Sci. 72 12 1472 1473 6363674 10.1002/jps.2600721227 1:CAS:528:DyaL2cXls1Orug%3D%3D (Pubitemid 14208330)
    • (1983) Journal of Pharmaceutical Sciences , vol.72 , Issue.12 , pp. 1472-1473
    • Quinn, R.1    Andrade, J.D.2
  • 10
    • 0027228385 scopus 로고
    • Techniques for assessing the effects of pharmaceutical excipients on the aggregation of porcine growth hormone
    • DOI 10.1023/A:1018994102218
    • SA Charman KL Mason WN Charman 1993 Techniques for assessing the effects of pharmaceutical excipients on the aggregation of porcine growth hormone Pharm Res. 10 7 954 962 8378257 10.1023/A:1018994102218 1:CAS:528:DyaK3sXlvVyntr8%3D (Pubitemid 23211415)
    • (1993) Pharmaceutical Research , vol.10 , Issue.7 , pp. 954-962
    • Charman, S.A.1    Mason, K.L.2    Charman, W.N.3
  • 11
    • 0342762048 scopus 로고    scopus 로고
    • Protein denaturation by combined effect of shear and air-liquid interface
    • DOI 10.1002/(SICI)1097-0290(19970620)54:6<503::AID-BIT1>3.0.CO;2-N
    • YF Maa CC Hsu 1997 Protein denaturation by combined effect of shear and air-liquid interface Biotechnol Bioeng. 54 6 503 512 18636406 10.1002/(SICI)1097-0290(19970620)54:6<503::AID-BIT1>3.0.CO;2-N 1:CAS:528:DyaK2sXjtVWqtbg%3D (Pubitemid 27209319)
    • (1997) Biotechnology and Bioengineering , vol.54 , Issue.6 , pp. 503-512
    • Maa, Y.-F.1    Hsu, C.C.2
  • 12
    • 0031391073 scopus 로고    scopus 로고
    • Use of poloxamer polymers to stabilize recombinant human growth hormone against various processing stresses
    • M Katakam AK Banga 1997 Use of poloxamer polymers to stabilize recombinant human growth hormone against various processing stresses Pharm Dev Technol. 2 2 143 149 9552440 10.3109/10837459709022619 1:CAS:528: DyaK2sXjvVygsbo%3D (Pubitemid 28252530)
    • (1997) Pharmaceutical Development and Technology , vol.2 , Issue.2 , pp. 143-149
    • Katakam, M.1    Banga, A.K.2
  • 13
    • 0029074530 scopus 로고
    • Effect of surfactants on the physical stability of recombinant human growth hormone
    • 7562409 10.1002/jps.2600840609 1:CAS:528:DyaK2MXlslyrsr4%3D
    • M Katakam LN Bell AK Banga 1995 Effect of surfactants on the physical stability of recombinant human growth hormone J Pharm Sci. 84 6 713 716 7562409 10.1002/jps.2600840609 1:CAS:528:DyaK2MXlslyrsr4%3D
    • (1995) J Pharm Sci. , vol.84 , Issue.6 , pp. 713-716
    • Katakam, M.1    Bell, L.N.2    Banga, A.K.3
  • 14
    • 0031742802 scopus 로고    scopus 로고
    • Tween protects recombinant human growth hormone against agitation- induced damage via hydrophobic interactions
    • DOI 10.1021/js980175v
    • NB Bam JL Cleland J Yang MC Manning JF Carpenter RF Kelley, et al. 1998 Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions J Pharm Sci. 87 12 1554 1559 10189266 10.1021/js980175v 1:CAS:528:DyaK1cXntVWlsbo%3D (Pubitemid 28559641)
    • (1998) Journal of Pharmaceutical Sciences , vol.87 , Issue.12 , pp. 1554-1559
    • Bam, N.B.1    Cleland, J.L.2    Yang, J.3    Manning, M.C.4    Carpenter, J.F.5    Kelley, R.F.6    Randolph, T.W.7
  • 15
    • 0002315499 scopus 로고
    • Use of a substituted cyclodextrin for stabilization of solutions of recombinant human growth hormone
    • M Hagenlocher R Pearlman 1989 Use of a substituted cyclodextrin for stabilization of solutions of recombinant human growth hormone Pharm Res. 6 S30
    • (1989) Pharm Res. , vol.6 , pp. 30
    • Hagenlocher, M.1    Pearlman, R.2
  • 16
    • 21344469442 scopus 로고    scopus 로고
    • Effects of Tween 20 and Tween 80 on the stability of Albutropin during agitation
    • DOI 10.1002/jps.20365
    • DK Chou R Krishnamurthy TW Randolph JF Carpenter MC Manning 2005 Effects of Tween 20 and Tween 80 on the stability of Albutropin during agitation J Pharm Sci. 94 6 1368 1381 15858848 10.1002/jps.20365 1:CAS:528:DC%2BD2MXkvF2qtbo%3D (Pubitemid 40904199)
    • (2005) Journal of Pharmaceutical Sciences , vol.94 , Issue.6 , pp. 1368-1381
    • Chou, D.K.1    Krishnamurthy, R.2    Randolph, T.W.3    Carpenter, J.F.4    Manning, M.C.5
  • 18
    • 55749109195 scopus 로고    scopus 로고
    • Shaken, not stirred: Mechanical stress testing of an IgG1 antibody
    • 18240293 10.1002/jps.21328 1:CAS:528:DC%2BD1cXht1Sgt7vF
    • S Kiese A Pappenberger W Friess HC Mahler 2008 Shaken, not stirred: mechanical stress testing of an IgG1 antibody J Pharm Sci. 97 10 4347 4366 18240293 10.1002/jps.21328 1:CAS:528:DC%2BD1cXht1Sgt7vF
    • (2008) J Pharm Sci. , vol.97 , Issue.10 , pp. 4347-4366
    • Kiese, S.1    Pappenberger, A.2    Friess, W.3    Mahler, H.C.4
  • 19
    • 76649084526 scopus 로고    scopus 로고
    • Inhibition of agitation-induced aggregation of an IgG-antibody by hydroxypropyl-beta-cyclodextrin
    • 19774651 1:CAS:528:DC%2BC3cXmvVGgtg%3D%3D
    • T Serno JF Carpenter TW Randolph G Winter 2010 Inhibition of agitation-induced aggregation of an IgG-antibody by hydroxypropyl-beta- cyclodextrin J Pharm Sci. 99 3 1193 1206 19774651 1:CAS:528: DC%2BC3cXmvVGgtg%3D%3D
    • (2010) J Pharm Sci. , vol.99 , Issue.3 , pp. 1193-1206
    • Serno, T.1    Carpenter, J.F.2    Randolph, T.W.3    Winter, G.4
  • 20
    • 68949136656 scopus 로고    scopus 로고
    • Silicone oil- and agitation-induced aggregation of a monoclonal antibody in aqueous solution
    • 19360857 10.1002/jps.21719 1:CAS:528:DC%2BD1MXptl2itrc%3D
    • R Thirumangalathu S Krishnan MS Ricci DN Brems TW Randolph JF Carpenter 2009 Silicone oil- and agitation-induced aggregation of a monoclonal antibody in aqueous solution J Pharm Sci. 98 9 3167 3181 19360857 10.1002/jps.21719 1:CAS:528:DC%2BD1MXptl2itrc%3D
    • (2009) J Pharm Sci. , vol.98 , Issue.9 , pp. 3167-3181
    • Thirumangalathu, R.1    Krishnan, S.2    Ricci, M.S.3    Brems, D.N.4    Randolph, T.W.5    Carpenter, J.F.6
  • 21
    • 68949103571 scopus 로고    scopus 로고
    • Adsorption and function of recombinant Factor VIII at the air-water interface in the presence of Tween 80
    • 18781611 10.1002/jps.21569 1:CAS:528:DC%2BD1MXptl2isbs%3D
    • O Joshi L Chu J McGuire DQ Wang 2009 Adsorption and function of recombinant Factor VIII at the air-water interface in the presence of Tween 80 J Pharm Sci. 98 9 3099 3107 18781611 10.1002/jps.21569 1:CAS:528: DC%2BD1MXptl2isbs%3D
    • (2009) J Pharm Sci. , vol.98 , Issue.9 , pp. 3099-3107
    • Joshi, O.1    Chu, L.2    McGuire, J.3    Wang, D.Q.4
  • 22
    • 0031773791 scopus 로고    scopus 로고
    • Effect of tween 20 on freeze-thawing- and agitation-induced aggregation of recombinant human factor XIII
    • L Kreilgaard LS Jones TW Randolph S Frokjaer JM Flink MC Manning, et al. 1998 Effect of Tween 20 on freeze-thawing- and agitation-induced aggregation of recombinant human factor XIII J Pharm Sci. 87 12 1597 1603 10189273 1:CAS:528:DyaK1cXmtlKgt78%3D (Pubitemid 28559648)
    • (1998) Journal of Pharmaceutical Sciences , vol.87 , Issue.12 , pp. 1597-1603
    • Kreilgaard, L.1
  • 23
    • 36549040103 scopus 로고    scopus 로고
    • Dual effects of Tween 80 on protein stability
    • DOI 10.1016/j.ijpharm.2007.06.042, PII S0378517307005212
    • W Wang YJ Wang DQ Wang 2008 Dual effects of Tween 80 on protein stability Int J Pharm. 347 1-2 31 38 17692480 10.1016/j.ijpharm.2007.06.042 1:CAS:528:DC%2BD2sXhtlOjsrnI (Pubitemid 350180316)
    • (2008) International Journal of Pharmaceutics , vol.347 , Issue.1-2 , pp. 31-38
    • Wang, W.1    Wang, Y.J.2    Wang, D.Q.3
  • 24
    • 0027876479 scopus 로고
    • Minimization of shaking-induced formation of insoluble aggregates of insulin by cyclodextrins
    • 8069577 10.3109/10611869308996093 1:CAS:528:DyaK2cXjtVOhtLc%3D
    • AK Banga R Mitra 1993 Minimization of shaking-induced formation of insoluble aggregates of insulin by cyclodextrins J Drug Target. 1 4 341 345 8069577 10.3109/10611869308996093 1:CAS:528:DyaK2cXjtVOhtLc%3D
    • (1993) J Drug Target. , vol.1 , Issue.4 , pp. 341-345
    • Banga, A.K.1    Mitra, R.2
  • 25
    • 77951266838 scopus 로고    scopus 로고
    • Formulation development of antibodies using robotic system and High-Throughput Laboratory (HTL)
    • 20014026 1:CAS:528:DC%2BC3cXjt1agt7o%3D
    • H Zhao O Graf N Milovic X Luan M Bluemel M Smolny, et al. 2010 Formulation development of antibodies using robotic system and High-Throughput Laboratory (HTL) J Pharm Sci. 99 5 2279 2294 20014026 1:CAS:528: DC%2BC3cXjt1agt7o%3D
    • (2010) J Pharm Sci. , vol.99 , Issue.5 , pp. 2279-2294
    • Zhao, H.1    Graf, O.2    Milovic, N.3    Luan, X.4    Bluemel, M.5    Smolny, M.6
  • 26
    • 57749185453 scopus 로고    scopus 로고
    • A high throughput protein formulation platform: Case study of salmon calcitonin
    • 18600433 10.1007/s11095-008-9662-8 1:CAS:528:DC%2BD1cXhsFSjsrzO
    • MA Capelle R Gurny T Arvinte 2009 A high throughput protein formulation platform: case study of salmon calcitonin Pharm Res. 26 1 118 128 18600433 10.1007/s11095-008-9662-8 1:CAS:528:DC%2BD1cXhsFSjsrzO
    • (2009) Pharm Res. , vol.26 , Issue.1 , pp. 118-128
    • Capelle, M.A.1    Gurny, R.2    Arvinte, T.3
  • 27
    • 78650570898 scopus 로고    scopus 로고
    • Application of extrinsic fluorescence spectroscopy for the high throughput formulation screening of aluminum-adjuvanted vaccines
    • 20740682 10.1002/jps.22282 1:CAS:528:DC%2BC3cXhs1ags7fP
    • SF Ausar J Chan W Hoque O James K Jayasundara K Harper 2011 Application of extrinsic fluorescence spectroscopy for the high throughput formulation screening of aluminum-adjuvanted vaccines J Pharm Sci. 100 2 431 440 20740682 10.1002/jps.22282 1:CAS:528:DC%2BC3cXhs1ags7fP
    • (2011) J Pharm Sci. , vol.100 , Issue.2 , pp. 431-440
    • Ausar, S.F.1    Chan, J.2    Hoque, W.3    James, O.4    Jayasundara, K.5    Harper, K.6
  • 28
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • 7108955 10.1016/0022-2836(82)90515-0 1:CAS:528:DyaL38Xks1yjtro%3D
    • J Kyte RF Doolittle 1982 A simple method for displaying the hydropathic character of a protein J Mol Biol. 157 1 105 132 7108955 10.1016/0022-2836(82) 90515-0 1:CAS:528:DyaL38Xks1yjtro%3D
    • (1982) J Mol Biol. , vol.157 , Issue.1 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 30
    • 0032502842 scopus 로고    scopus 로고
    • Multichannel pipettor performance verified by measuring pathlength of reagent dispensed into a microplate
    • DOI 10.1006/abio.1998.2621
    • EL McGown DG Hafeman 1998 Multichannel pipettor performance verified by measuring pathlength of reagent dispensed into a microplate Anal Biochem. 258 1 155 157 9527867 10.1006/abio.1998.2621 1:CAS:528:DyaK1cXitlKhsLs%3D (Pubitemid 28163162)
    • (1998) Analytical Biochemistry , vol.258 , Issue.1 , pp. 155-157
    • McGown, E.L.1    Hafeman, D.G.2
  • 31
    • 33646196840 scopus 로고    scopus 로고
    • Evaluation of the information content in infrared spectra for protein secondary structure determination
    • 16428280 10.1529/biophysj.105.072017 1:CAS:528:DC%2BD28XjsFequrg%3D
    • E Goormaghtigh JM Ruysschaert V Raussens 2006 Evaluation of the information content in infrared spectra for protein secondary structure determination Biophys J. 90 8 2946 2957 16428280 10.1529/biophysj.105.072017 1:CAS:528:DC%2BD28XjsFequrg%3D
    • (2006) Biophys J. , vol.90 , Issue.8 , pp. 2946-2957
    • Goormaghtigh, E.1    Ruysschaert, J.M.2    Raussens, V.3
  • 32
    • 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
    • DOI 10.1021/js950332f
    • BS Kendrick A Dong SD Allison MC Manning JF Carpenter 1996 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 2 155 158 8683440 10.1021/js950332f 1:CAS:528:DyaK28XjtFyisg%3D%3D (Pubitemid 26055795)
    • (1996) Journal of Pharmaceutical Sciences , vol.85 , Issue.2 , pp. 155-158
    • Kendrick, B.S.1    Dong, A.2    Allison, S.D.3    Manning, M.C.4    Carpenter, J.F.5
  • 34
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • DOI 10.1177/108705719900400206
    • JH Zhang TD Chung KR Oldenburg 1999 A simple statistical parameter for use in evaluation and validation of high throughput screening assays J Biomol Screen. 4 2 67 73 10838414 10.1177/108705719900400206 (Pubitemid 29278954)
    • (1999) Journal of Biomolecular Screening , vol.4 , Issue.2 , pp. 67-73
    • Zhang, J.-H.1    Chung, T.D.Y.2    Oldenburg, K.R.3
  • 35
    • 0023476453 scopus 로고
    • Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces
    • 3442318 10.1016/0003-2697(87)90157-6 1:CAS:528:DyaL1cXhvVKqtw%3D%3D
    • DL Sackett J Wolff 1987 Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces Anal Biochem. 167 2 228 234 3442318 10.1016/0003-2697(87)90157-6 1:CAS:528:DyaL1cXhvVKqtw%3D%3D
    • (1987) Anal Biochem. , vol.167 , Issue.2 , pp. 228-234
    • Sackett, D.L.1    Wolff, J.2
  • 37
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • 3697478 10.1002/bip.360250307 1:CAS:528:DyaL28Xht1GqtLc%3D
    • DM Byler H Susi 1986 Examination of the secondary structure of proteins by deconvolved FTIR spectra Biopolymers. 25 3 469 487 3697478 10.1002/bip.360250307 1:CAS:528:DyaL28Xht1GqtLc%3D
    • (1986) Biopolymers. , vol.25 , Issue.3 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 38
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • A Dong P Huang WS Caughey 1990 Protein secondary structures in water from second-derivative amide I infrared spectra Biochemistry. 29 13 3303 3308 2159334 10.1021/bi00465a022 1:CAS:528:DyaK3cXhsFCltrg%3D (Pubitemid 20131472)
    • (1990) Biochemistry , vol.29 , Issue.13 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 39
    • 0003022686 scopus 로고    scopus 로고
    • Determining the fluorescence spectrum of a protein
    • 7.7.1-7.7.20
    • Pain RH. Determining the fluorescence spectrum of a protein. Curr Protoc Protein Sci. 2004;S38:7.7.1-7.7.20.
    • (2004) Curr Protoc Protein Sci.
    • Pain, R.H.1
  • 40
    • 77951267552 scopus 로고    scopus 로고
    • Potential inaccurate quantitation and sizing of protein aggregates by size exclusion chromatography: Essential need to use orthogonal methods to assure the quality of therapeutic protein products
    • 19918982 10.1002/jps.21989 1:CAS:528:DC%2BC3cXjt1ahurg%3D
    • JF Carpenter TW Randolph W Jiskoot DJ Crommelin CR Middaugh G Winter 2010 Potential inaccurate quantitation and sizing of protein aggregates by size exclusion chromatography: essential need to use orthogonal methods to assure the quality of therapeutic protein products J Pharm Sci. 99 5 2200 2208 19918982 10.1002/jps.21989 1:CAS:528:DC%2BC3cXjt1ahurg%3D
    • (2010) J Pharm Sci. , vol.99 , Issue.5 , pp. 2200-2208
    • Carpenter, J.F.1    Randolph, T.W.2    Jiskoot, W.3    Crommelin, D.J.4    Middaugh, C.R.5    Winter, G.6
  • 41
    • 75349114023 scopus 로고    scopus 로고
    • Recent trends in stabilising peptides and proteins in pharmaceutical formulation - Considerations in the choice of excipients
    • 19678792 10.1517/17425240903199143 1:CAS:528:DC%2BD1MXhtlWlsLfJ
    • L Jorgensen S Hostrup EH Moeller H Grohganz 2009 Recent trends in stabilising peptides and proteins in pharmaceutical formulation - considerations in the choice of excipients Expert Opin Drug Deliv. 6 11 1219 1230 19678792 10.1517/17425240903199143 1:CAS:528:DC%2BD1MXhtlWlsLfJ
    • (2009) Expert Opin Drug Deliv. , vol.6 , Issue.11 , pp. 1219-1230
    • Jorgensen, L.1    Hostrup, S.2    Moeller, E.H.3    Grohganz, H.4
  • 42
    • 77951605340 scopus 로고    scopus 로고
    • The effects of substituted cyclodextrins on the colloidal and conformational stability of selected proteins
    • 20049940 1:CAS:528:DC%2BC3cXkvVOkurg%3D
    • HS Samra F He A Bhambhani JD Pipkin R Zimmerer SB Joshi, et al. 2010 The effects of substituted cyclodextrins on the colloidal and conformational stability of selected proteins J Pharm Sci. 99 6 2800 2818 20049940 1:CAS:528:DC%2BC3cXkvVOkurg%3D
    • (2010) J Pharm Sci. , vol.99 , Issue.6 , pp. 2800-2818
    • Samra, H.S.1    He, F.2    Bhambhani, A.3    Pipkin, J.D.4    Zimmerer, R.5    Joshi, S.B.6
  • 43
    • 0006125101 scopus 로고
    • Availability of drugs in the presence of surface-active agents. I. Critical micelle concentrations of some oxyethylene oxypropylene polymers
    • 14288499 10.1002/jps.2600540117 1:CAS:528:DyaF2MXltVOrsw%3D%3D
    • W Saski SG Shah 1965 Availability of drugs in the presence of surface-active agents. I. Critical micelle concentrations of some oxyethylene oxypropylene polymers J Pharm Sci. 54 71 74 14288499 10.1002/jps.2600540117 1:CAS:528:DyaF2MXltVOrsw%3D%3D
    • (1965) J Pharm Sci. , vol.54 , pp. 71-74
    • Saski, W.1    Shah, S.G.2
  • 44
    • 0020696718 scopus 로고
    • Ultrasonic velocity and light-scattering studies on the polyoxyethylene-polyoxypropylene copolymer Pluronic F127 in aqueous solution
    • DOI 10.1016/0378-5173(82)90141-7
    • J Rassing D Attwood 1982 Ultrasonic velocity and light-scattering studies on the polyoxyethylene-polyoxypropylene copolymer Pluronic F127 in aqueous solution Int J Pharm. 13 1 47 55 10.1016/0378-5173(82)90141-7 1:CAS:528:DyaL3sXnvVSnuw%3D%3D (Pubitemid 13221124)
    • (1983) International Journal of Pharmaceutics , vol.13 , Issue.1 , pp. 47-55
    • Rassing, J.1    Attwood, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.