메뉴 건너뛰기




Volumn 6, Issue 1, 2015, Pages 59-82

Solid-state protein formulations

Author keywords

[No Author keywords available]

Indexed keywords

MONOCLONAL ANTIBODY; PROTEIN DERIVATIVE; PROTEIN;

EID: 84920711952     PISSN: 20415990     EISSN: 20416008     Source Type: Journal    
DOI: 10.4155/tde.14.98     Document Type: Review
Times cited : (32)

References (148)
  • 2
    • 40049100326 scopus 로고    scopus 로고
    • Protein folding, unfolding and misfolding: Role played by intermediate states
    • Santucci R, Sinibaldi F, Fiorucci L. Protein folding, unfolding and misfolding: role played by intermediate states. Mini Rev. Med. Chem. 8(1), 57-62 (2008).
    • (2008) Mini Rev. Med. Chem. , vol.8 , Issue.1 , pp. 57-62
    • Santucci, R.1    Sinibaldi, F.2    Fiorucci, L.3
  • 3
    • 0025179832 scopus 로고
    • Protein folding
    • Creighton T. Protein folding. Biochem. J. 270(1), 1-16 (1990).
    • (1990) Biochem. J. , vol.270 , Issue.1 , pp. 1-16
    • Creighton, T.1
  • 4
    • 84869761071 scopus 로고    scopus 로고
    • The protein-folding problem, 50 years on
    • Dill KA, MacCallum JL. The protein-folding problem, 50 years on. Science 338 (6110), 1042-1046 (2012).
    • (2012) Science , vol.338 , Issue.6110 , pp. 1042-1046
    • Dill, K.A.1    MacCallum, J.L.2
  • 6
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: A formulation challenge
    • Frokjaer S, Otzen DE. Protein drug stability: a formulation challenge. Nat. Rev. Drug Discov. 4(4), 298-306 (2005).
    • (2005) Nat. Rev. Drug Discov. , vol.4 , Issue.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 7
    • 0024806396 scopus 로고
    • Stability of protein pharmaceuticals
    • Manning MC, Patel K, Borchardt RT. Stability of protein pharmaceuticals. Pharm. Res. 6(11), 903-918 (1989).
    • (1989) Pharm. Res. , vol.6 , Issue.11 , pp. 903-918
    • Manning, M.C.1    Patel, K.2    Borchardt, R.T.3
  • 8
    • 33646871008 scopus 로고    scopus 로고
    • Metastable, partially folded states in the productive folding and in the misfolding and amyloid aggregation of proteins
    • Ferreira ST, De Felice FG, Chapeaurouge A. Metastable, partially folded states in the productive folding and in the misfolding and amyloid aggregation of proteins. Cell Biochem. Biophys. 44(3), 539-548 (2006).
    • (2006) Cell Biochem. Biophys. , vol.44 , Issue.3 , pp. 539-548
    • Ferreira, S.T.1    De Felice, F.G.2    Chapeaurouge, A.3
  • 9
    • 84860013075 scopus 로고    scopus 로고
    • Structure of an intermediate state in protein folding and aggregation
    • Neudecker P, Robustelli P, Cavalli A et al. Structure of an intermediate state in protein folding and aggregation. Science 336(6079), 362-366 (2012).
    • (2012) Science , vol.336 , Issue.6079 , pp. 362-366
    • Neudecker, P.1    Robustelli, P.2    Cavalli, A.3
  • 10
    • 12544259221 scopus 로고    scopus 로고
    • Reversal of protein aggregation provides evidence for multiple aggregated States
    • Calamai M, Canale C, Relini A, Stefani M, Chiti F, Dobson CM. Reversal of protein aggregation provides evidence for multiple aggregated States. J. Mol. Biol. 346(2), 603-616 (2005).
    • (2005) J. Mol. Biol. , vol.346 , Issue.2 , pp. 603-616
    • Calamai, M.1    Canale, C.2    Relini, A.3    Stefani, M.4    Chiti, F.5    Dobson, C.M.6
  • 13
    • 84876481833 scopus 로고    scopus 로고
    • Effect of pH and excipients on structure, dynamics, and long-term stability of a model IgG1 monoclonal antibody upon freeze-drying
    • Park J, Nagapudi K, Vergara C, Ramachander R, Laurence JS, Krishnan S. Effect of pH and excipients on structure, dynamics, and long-term stability of a model IgG1 monoclonal antibody upon freeze-drying. Pharm. Res. 30(4), 968-984 (2013).
    • (2013) Pharm. Res. , vol.30 , Issue.4 , pp. 968-984
    • Park, J.1    Nagapudi, K.2    Vergara, C.3    Ramachander, R.4    Laurence, J.S.5    Krishnan, S.6
  • 14
    • 77951498805 scopus 로고    scopus 로고
    • Protein aggregation-pathways and infuencing factors
    • Wang W, Nema S, Teagarden D. Protein aggregation-pathways and infuencing factors. Int. J. Pharm. 390(2), 89-99 (2010).
    • (2010) Int. J. Pharm. , vol.390 , Issue.2 , pp. 89-99
    • Wang, W.1    Nema, S.2    Teagarden, D.3
  • 15
    • 84903216265 scopus 로고    scopus 로고
    • Freezing-induced perturbation of tertiary structure of a monoclonal antibody
    • Liu L, Braun LJ, Wang W, Randolph TW, Carpenter JF. Freezing-induced perturbation of tertiary structure of a monoclonal antibody. J. Pharm. Sci. 103 (7), 1979-1986 (2014).
    • (2014) J. Pharm. Sci. , vol.103 , Issue.7 , pp. 1979-1986
    • Liu, L.1    Braun, L.J.2    Wang, W.3    Randolph, T.W.4    Carpenter, J.F.5
  • 16
    • 84863070501 scopus 로고    scopus 로고
    • Salting effects on protein components in aqueous NaCl and urea solutions: Toward understanding of urea-induced protein denaturation
    • Li W, Zhou R, Mu Y. Salting effects on protein components in aqueous NaCl and urea solutions: toward understanding of urea-induced protein denaturation. J. Phys. Chem. B. 116 (4), 1446-1451 (2012).
    • (2012) J. Phys. Chem. B. , vol.116 , Issue.4 , pp. 1446-1451
    • Li, W.1    Zhou, R.2    Mu, Y.3
  • 17
    • 0028569153 scopus 로고
    • Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
    • Monera OD, Kay CM, Hodges RS. Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3(11), 1984-1991 (1994).
    • (1994) Protein Sci. , vol.3 , Issue.11 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 18
    • 68949085124 scopus 로고    scopus 로고
    • Protein aggregation: Pathways, induction factors and analysis
    • Mahler H-C, Friess W, Grauschopf U, Kiese S. Protein aggregation: pathways, induction factors and analysis. J. Pharm. Sci. 98(9), 2909-2934 (2009).
    • (2009) J. Pharm. Sci. , vol.98 , Issue.9 , pp. 2909-2934
    • Mahler, H.-C.1    Friess, W.2    Grauschopf, U.3    Kiese, S.4
  • 19
    • 27644477360 scopus 로고    scopus 로고
    • Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution
    • Liu J, Nguyen MDH, Andya JD, Shire SJ. Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution. J. Pharm. Sci. 94 (9), 1928-1940 (2005).
    • (2005) J. Pharm. Sci. , vol.94 , Issue.9 , pp. 1928-1940
    • Liu, J.1    Nguyen, M.D.H.2    Andya, J.D.3    Shire, S.J.4
  • 20
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W. Protein aggregation and its inhibition in biopharmaceutics. Int. J. Pharm. 289(1-2), 1-30 (2005).
    • (2005) Int. J. Pharm. , vol.289 , Issue.1-2 , pp. 1-30
    • Wang, W.1
  • 21
    • 3042761213 scopus 로고    scopus 로고
    • Structure-immunogenicity relationships of therapeutic proteins
    • Hermeling S, Crommelin DJA, Schellekens H, Jiskoot W. Structure-immunogenicity relationships of therapeutic proteins. Pharm. Res. 21(6), 897-903 (2004).
    • (2004) Pharm. Res. , vol.21 , Issue.6 , pp. 897-903
    • Hermeling, S.1    Crommelin, D.J.A.2    Schellekens, H.3    Jiskoot, W.4
  • 22
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An immunologic perspective
    • Rosenberg AS. Effects of protein aggregates: an immunologic perspective. AAPS J. 8(3), E501-E507 (2006).
    • (2006) AAPS J. , vol.8 , Issue.3 , pp. E501-E507
    • Rosenberg, A.S.1
  • 23
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani M, Dobson CM. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81(11), 678-699 (2003).
    • (2003) J. Mol. Med. , vol.81 , Issue.11 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 24
    • 80054717076 scopus 로고    scopus 로고
    • Protein-excipient interactions: Mechanisms and biophysical characterization applied to protein formulation development
    • Kamerzell TJ, Esfandiary R, Joshi SB, Middaugh CR, Volkin DB. Protein-excipient interactions: mechanisms and biophysical characterization applied to protein formulation development. Adv. Drug Deliv. Rev. 63(13), 1118-1159 (2011).
    • (2011) Adv. Drug Deliv. Rev. , vol.63 , Issue.13 , pp. 1118-1159
    • Kamerzell, T.J.1    Esfandiary, R.2    Joshi, S.B.3    Middaugh, C.R.4    Volkin, D.B.5
  • 25
    • 84874411132 scopus 로고    scopus 로고
    • Analytical methods and formulation factors to enhance protein stability in solution
    • Jeong SH. Analytical methods and formulation factors to enhance protein stability in solution. Arch. Pharm. Res. 35(11), 1871-1886 (2012).
    • (2012) Arch. Pharm. Res. , vol.35 , Issue.11 , pp. 1871-1886
    • Jeong, S.H.1
  • 26
    • 80052268214 scopus 로고    scopus 로고
    • Multidimensional methods for the formulation of biopharmaceuticals and vaccines
    • Maddux NR, Joshi SB, Volkin DB, Ralston JP, Middaugh CR. Multidimensional methods for the formulation of biopharmaceuticals and vaccines. J. Pharm. Sci. 100(10), 4171-4197 (2011).
    • (2011) J. Pharm. Sci. , vol.100 , Issue.10 , pp. 4171-4197
    • Maddux, N.R.1    Joshi, S.B.2    Volkin, D.B.3    Ralston, J.P.4    Middaugh, C.R.5
  • 27
    • 84886075107 scopus 로고    scopus 로고
    • Development of formulations for therapeutic monoclonal antibodies and Fc fusion proteins
    • Jameel F, Hershenson S (Eds.). John Wiley & Sons Inc., Hoboken, NJ, USA
    • Krishnan S, Pallitto M, Ricci M. Development of formulations for therapeutic monoclonal antibodies and Fc fusion proteins. In: Formulation and Process Development Strategies for Manufacturing Biopharmaceuticals. Jameel F, Hershenson S (Eds.). John Wiley & Sons Inc., Hoboken, NJ, USA, 383-428 (2010).
    • (2010) Formulation and Process Development Strategies for Manufacturing Biopharmaceuticals , pp. 383-428
    • Krishnan, S.1    Pallitto, M.2    Ricci, M.3
  • 28
    • 84858792435 scopus 로고    scopus 로고
    • Calorimetry and complementary techniques to characterize frozen and freeze-dried systems
    • Sundaramurthi P, Suryanarayanan R. Calorimetry and complementary techniques to characterize frozen and freeze-dried systems. Adv. Drug Deliv. Rev. 64(5), 384-395 (2012).
    • (2012) Adv. Drug Deliv. Rev. , vol.64 , Issue.5 , pp. 384-395
    • Sundaramurthi, P.1    Suryanarayanan, R.2
  • 30
    • 55449104956 scopus 로고    scopus 로고
    • Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations
    • Andya JD, Hsu CC, Shire SJ. Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations. AAPS PharmSci. 5(2), 21-31 (2003).
    • (2003) AAPS PharmSci. , vol.5 , Issue.2 , pp. 21-31
    • Andya, J.D.1    Hsu, C.C.2    Shire, S.J.3
  • 31
    • 0032078241 scopus 로고    scopus 로고
    • Freeze-drying of bioproducts: Putting principles into practice
    • Franks F. Freeze-drying of bioproducts: putting principles into practice. Eur. J. Pharm. Biopharm. 45(3), 221-229 (1998).
    • (1998) Eur. J. Pharm. Biopharm. , vol.45 , Issue.3 , pp. 221-229
    • Franks, F.1
  • 32
    • 0030770631 scopus 로고    scopus 로고
    • Randolph TW Rational design of stable lyophilized protein formulations: Some practical advice
    • Carpenter JF, Pikal MJ, Chang BS, Randolph TW Rational design of stable lyophilized protein formulations: some practical advice. Pharm. Res. 14(8), 969-975 (1997).
    • (1997) Pharm. Res. , vol.14 , Issue.8 , pp. 969-975
    • Carpenter, J.F.1    Pikal, M.J.2    Chang, B.S.3
  • 33
    • 85153887742 scopus 로고    scopus 로고
    • Physical forms I-Crystalline materials
    • John Wiley & Sons Inc., West Sussex
    • Gaisford S, Saunders M. Physical forms I-Crystalline materials. In: Essentials of Pharmaceutical Preformulation. John Wiley & Sons Inc., West Sussex, 127-155 (2013).
    • (2013) Essentials of Pharmaceutical Preformulation , pp. 127-155
    • Gaisford, S.1    Saunders, M.2
  • 36
    • 38749149916 scopus 로고    scopus 로고
    • Protein crystallization: From purifed protein to diffraction-quality crystal
    • Chayen NE, Saridakis E. Protein crystallization: from purifed protein to diffraction-quality crystal. Nat. Method. 5(2), 147-153 (2008).
    • (2008) Nat. Method. , vol.5 , Issue.2 , pp. 147-153
    • Chayen, N.E.1    Saridakis, E.2
  • 37
    • 0022335486 scopus 로고
    • Nucleation and growth of protein crystals: General principles and assays
    • Feher G, Kam Z. Nucleation and growth of protein crystals: general principles and assays. Methods Enzymol. 114, 77-112 (1985).
    • (1985) Methods Enzymol. , vol.114 , pp. 77-112
    • Feher, G.1    Kam, Z.2
  • 38
    • 37049223385 scopus 로고
    • The infuence of nickel and cobalt on the effect exerted by insulin in a rabbit
    • Bertrand G, Macheboeuf M. The infuence of nickel and cobalt on the effect exerted by insulin in a rabbit. Science 64, 629-630 (1926).
    • (1926) Science , vol.64 , pp. 629-630
    • Bertrand, G.1    MacHeboeuf, M.2
  • 39
    • 0345541017 scopus 로고
    • The normal occurrence of zinc in biologic materials: A review of the literature, and a study of the normal distribution of zinc in the rat, cat, and man
    • Lutz RE. The normal occurrence of zinc in biologic materials: a review of the literature, and a study of the normal distribution of zinc in the rat, cat, and man. J. Ind. Hygiene 8, 177 (1926).
    • (1926) J. Ind. Hygiene , vol.8 , pp. 177
    • Lutz, R.E.1
  • 42
    • 0028849027 scopus 로고
    • X-ray crystallographic studies on hexameric insulins in the presence of helix-stabilizing agenst, thiocyanate, methylparaben and phenol
    • Whittingham JL, Chaudhuri S, Dodson EJ, Moody PC, Dodson GG. X-ray crystallographic studies on hexameric insulins in the presence of helix-stabilizing agenst, thiocyanate, methylparaben and phenol. Biochemistry 34, 15553-15563 (1995).
    • (1995) Biochemistry , vol.34 , pp. 15553-15563
    • Whittingham, J.L.1    Chaudhuri, S.2    Dodson, E.J.3    Moody, P.C.4    Dodson, G.G.5
  • 43
    • 0026955771 scopus 로고
    • Structure of a rhombohedral R6 insulin/phenol complex
    • Smith GD, Dodson GG. Structure of a rhombohedral R6 insulin/phenol complex. Proteins 14, 401-408 (1992).
    • (1992) Proteins , vol.14 , pp. 401-408
    • Smith, G.D.1    Dodson, G.G.2
  • 44
    • 84881326162 scopus 로고    scopus 로고
    • Characterization of physiochemical and biological properties of spherical protein crystals for sustained release
    • Shi K, Bi H, Jiang Y. Characterization of physiochemical and biological properties of spherical protein crystals for sustained release. Asian J. Pharm. Sci. 8(1), 58-63 (2013).
    • (2013) Asian J. Pharm. Sci. , vol.8 , Issue.1 , pp. 58-63
    • Shi, K.1    Bi, H.2    Jiang, Y.3
  • 45
    • 84880354946 scopus 로고    scopus 로고
    • Stirred batch crystallization of a therapeutic antibody fragment
    • Hebel D, Huber S, Stanislawski B, Hekmat D. Stirred batch crystallization of a therapeutic antibody fragment. J. Biotechnol. 166, 206-211 (2013).
    • (2013) J. Biotechnol. , vol.166 , pp. 206-211
    • Hebel, D.1    Huber, S.2    Stanislawski, B.3    Hekmat, D.4
  • 46
    • 55349139343 scopus 로고    scopus 로고
    • How do crystal lattice contacts reveal protein crystallization mechanism?
    • Nanev CN. How do crystal lattice contacts reveal protein crystallization mechanism? Cryst. Res. Technol. 43(9), 914-920 (2008).
    • (2008) Cryst. Res. Technol. , vol.43 , Issue.9 , pp. 914-920
    • Nanev, C.N.1
  • 47
    • 33846492434 scopus 로고    scopus 로고
    • Protein crystal nucleation: Recent notions
    • Nanev CN. Protein crystal nucleation: Recent notions. Cryst. Res. Technol. 42(1), 4-12 (2007).
    • (2007) Cryst. Res. Technol. , vol.42 , Issue.1 , pp. 4-12
    • Nanev, C.N.1
  • 48
    • 0026607545 scopus 로고
    • Kinetics of protein-protein association explained by Brownian dynamics computer simulation
    • Northrup SH, Erickson HP. Kinetics of protein-protein association explained by Brownian dynamics computer simulation. Proc. Natl Acad. Sci. USA 89(8), 3338-3342 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , Issue.8 , pp. 3338-3342
    • Northrup, S.H.1    Erickson, H.P.2
  • 49
    • 0028787430 scopus 로고
    • Yeates T Why protein crystals favour some space-groups over others
    • Wukovitz S, Yeates T Why protein crystals favour some space-groups over others. Nat. Struc. Biol. 2, 1062-1067 (1995).
    • (1995) Nat. Struc. Biol. , vol.2 , pp. 1062-1067
    • Wukovitz, S.1
  • 50
    • 33846492434 scopus 로고    scopus 로고
    • Protein crystal nucleation: Recent notions
    • Nanev CN. Protein crystal nucleation: Recent notions. Crystal Res. Tech. 12(1), 4-12 (2007).
    • (2007) Crystal Res. Tech. , vol.12 , Issue.1 , pp. 4-12
    • Nanev, C.N.1
  • 51
    • 84887445471 scopus 로고    scopus 로고
    • Kinetics and intimate mechanism of protein crystal nucleation
    • Nanev CN. Kinetics and intimate mechanism of protein crystal nucleation. Prog. Cryst. Growth Charact. Mater. 59(4), 133-169 (2013).
    • (2013) Prog. Cryst. Growth Charact. Mater. , vol.59 , Issue.4 , pp. 133-169
    • Nanev, C.N.1
  • 52
    • 33750610316 scopus 로고    scopus 로고
    • Chemical and thermal stability of insulin: Effects of zinc and ligand binding to the insulin zinc-hexamer
    • Huus K, Havelund S, Olsen HB, van de Wert M, Frokjaer S. Chemical and thermal stability of insulin: effects of zinc and ligand binding to the insulin zinc-hexamer. Pharm. Res. 23(11), 2611-2620 (2006).
    • (2006) Pharm. Res. , vol.23 , Issue.11 , pp. 2611-2620
    • Huus, K.1    Havelund, S.2    Olsen, H.B.3    Van De Wert, M.4    Frokjaer, S.5
  • 53
    • 0035448570 scopus 로고    scopus 로고
    • Insulins today and beyond
    • Owens DR, Zinman B, Bolli GB. Insulins today and beyond. Lancet 358(9283), 739-46 (2001).
    • (2001) Lancet , vol.358 , Issue.9283 , pp. 739-746
    • Owens, D.R.1    Zinman, B.2    Bolli, G.B.3
  • 54
    • 17844366885 scopus 로고    scopus 로고
    • Therapeutic insulins and their large-scale manufacture
    • Walsh G. Therapeutic insulins and their large-scale manufacture. Appl. Microbiol. Biotechnol. 67(2), 151-159 (2005).
    • (2005) Appl. Microbiol. Biotechnol. , vol.67 , Issue.2 , pp. 151-159
    • Walsh, G.1
  • 55
    • 84864460325 scopus 로고    scopus 로고
    • Design of the novel protraction mechanism of insulin degludec, an ultra-long-acting basal insulin
    • Jonassen I, Havelund S, Jensen T, Steensgaard D, Wahlund P, Ribel U. Design of the novel protraction mechanism of insulin degludec, an ultra-long-acting basal insulin. Pharm. Res. 29, 2104-2114 (2012).
    • (2012) Pharm. Res. , vol.29 , pp. 2104-2114
    • Jonassen, I.1    Havelund, S.2    Jensen, T.3    Steensgaard, D.4    Wahlund, P.5    Ribel, U.6
  • 57
    • 0025509402 scopus 로고
    • Purifcation and analysis of the major components of chum salmon protamine contained in insulin formulations using high-performance liquid chromatography
    • Hoffmann J, Chance R, Johnson M. Purifcation and analysis of the major components of chum salmon protamine contained in insulin formulations using high-performance liquid chromatography. Protein Expr. Purif. 1(2), 127-133 (1990).
    • (1990) Protein Expr. Purif. , vol.1 , Issue.2 , pp. 127-133
    • Hoffmann, J.1    Chance, R.2    Johnson, M.3
  • 59
    • 33947261481 scopus 로고    scopus 로고
    • Structural characterization of insulin NPH formulations
    • Norrman M, Hubálek F, Schluckebier G. Structural characterization of insulin NPH formulations. Eur. J. Pharm. Sci. 30(5), 414-423 (2007).
    • (2007) Eur. J. Pharm. Sci. , vol.30 , Issue.5 , pp. 414-423
    • Norrman, M.1    Hubálek, F.2    Schluckebier, G.3
  • 60
    • 11844250564 scopus 로고    scopus 로고
    • Insulin analogues
    • Hirsch I. Insulin analogues. N. Engl. J. Med. 352, 174-183 (2005).
    • (2005) N. Engl. J. Med. , vol.352 , pp. 174-183
    • Hirsch, I.1
  • 61
    • 0031033686 scopus 로고    scopus 로고
    • Insulin analogues
    • Barnett A, Owens D. Insulin analogues. Lancet 349 (9044), 47-51 (1997).
    • (1997) Lancet , vol.349 , Issue.9044 , pp. 47-51
    • Barnett, A.1    Owens, D.2
  • 62
    • 84874326976 scopus 로고    scopus 로고
    • Insulin degludec: Overview of a novel ultra long-acting basal insulin
    • Gough SCL, Harris S, Woo V, Davies M. Insulin degludec: overview of a novel ultra long-acting basal insulin. Diabetes. O bes. Metab. 15(4), 301-309 (2013).
    • (2013) Diabetes. O Bes. Metab. , vol.15 , Issue.4 , pp. 301-309
    • Gough, S.C.L.1    Harris, S.2    Woo, V.3    Davies, M.4
  • 64
    • 0037154268 scopus 로고    scopus 로고
    • Protein folding mediated by solvation: Water expulsion and formation of the hydrophobic core occur after the structural collapse
    • Cheung MS, García AE, Onuchic JN. Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse. Proc. Natl Acad. Sci. USA 99(2), 685-690 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.2 , pp. 685-690
    • Cheung, M.S.1    García, A.E.2    Onuchic, J.N.3
  • 65
    • 85051765641 scopus 로고    scopus 로고
    • Formulation of biotech products, including biopharmaceutical considerations
    • Crommelin DJA, Sindelar RD, Meibohm B (Eds.). Springer, New York, USA
    • Crommelin DJ. Formulation of biotech products, including biopharmaceutical considerations. In: Pharmaceutical Biotechnology. Crommelin DJA, Sindelar RD, Meibohm B (Eds.). Springer, New York, USA, 67-123 (2008).
    • (2008) Pharmaceutical Biotechnology , pp. 67-123
    • Crommelin, D.J.1
  • 66
    • 79955874261 scopus 로고    scopus 로고
    • The freezing step in lyophilization: Physico-chemical fundamentals, freezing methods and consequences on process performance and quality attributes of biopharmaceuticals
    • Kasper JC, Friess W. The freezing step in lyophilization: physico-chemical fundamentals, freezing methods and consequences on process performance and quality attributes of biopharmaceuticals. Eur. J. Pharm. Biopharm. 78(2), 248-63 (2011).
    • (2011) Eur. J. Pharm. Biopharm. , vol.78 , Issue.2 , pp. 248-263
    • Kasper, J.C.1    Friess, W.2
  • 67
    • 0034255393 scopus 로고    scopus 로고
    • Lyophilization and development of solid protein pharmaceuticals
    • Wang W Lyophilization and development of solid protein pharmaceuticals. Int. J. Pharm. 203(1-2), 1-60 (2000).
    • (2000) Int. J. Pharm. , vol.203 , Issue.1-2 , pp. 1-60
    • Wang, W.1
  • 68
    • 0033586786 scopus 로고    scopus 로고
    • Protein formulation and lyophilization cycle design: Prevention of damage due to freeze-concentration induced phase separation
    • Heller MC, Carpenter JF, Randolph TW Protein formulation and lyophilization cycle design: Prevention of damage due to freeze-concentration induced phase separation. Biotechnol. Bioeng. 63(2), 166-174 (1999).
    • (1999) Biotechnol. Bioeng. , vol.63 , Issue.2 , pp. 166-174
    • Heller, M.C.1    Carpenter, J.F.2    Randolph, T.W.3
  • 69
    • 1242314686 scopus 로고    scopus 로고
    • Design of freeze-drying processes for pharmaceuticals: Practical advice
    • Tang X, Pikal MJ. Design of freeze-drying processes for pharmaceuticals: practical advice. Pharm. Res. 21(2), 191-200 (2004).
    • (2004) Pharm. Res. , vol.21 , Issue.2 , pp. 191-200
    • Tang, X.1    Pikal, M.J.2
  • 70
    • 34250738378 scopus 로고    scopus 로고
    • Lyophilization cycle development for a high-concentration monoclonal antibody formulation lacking a crystalline bulking agent
    • Colandene JD, Maldonado LM, Creagh AT, Vrettos JS, Goad KG, Spitznagel TM. Lyophilization cycle development for a high-concentration monoclonal antibody formulation lacking a crystalline bulking agent. J. Pharm. Sci. 96(6), 1598-1608 (2007).
    • (2007) J. Pharm. Sci. , vol.96 , Issue.6 , pp. 1598-1608
    • Colandene, J.D.1    Maldonado, L.M.2    Creagh, A.T.3    Vrettos, J.S.4    Goad, K.G.5    Spitznagel, T.M.6
  • 72
    • 68949085125 scopus 로고    scopus 로고
    • Mechanisms of protein stabilization in the solid state
    • Chang LL, Pikal MJ. Mechanisms of protein stabilization in the solid state. J. Pharm. Sci. 98(9), 2886-2908 (2009).
    • (2009) J. Pharm. Sci. , vol.98 , Issue.9 , pp. 2886-2908
    • Chang, L.L.1    Pikal, M.J.2
  • 73
    • 0025952279 scopus 로고
    • Effect of freezing on aggregation of human growth hormone
    • Eckhardt BM, Oeswein JQ, Bewley TA. Effect of freezing on aggregation of human growth hormone. Pharm. Res. 8(11), 1360-1364 (1991).
    • (1991) Pharm. Res. , vol.8 , Issue.11 , pp. 1360-1364
    • Eckhardt, B.M.1    Oeswein, J.Q.2    Bewley, T.A.3
  • 74
    • 0030043206 scopus 로고    scopus 로고
    • Proteins in frozen solutions: Evidence of ice-induced partial unfolding
    • Strambini GB, Gabellieri E. Proteins in frozen solutions: evidence of ice-induced partial unfolding. Biophys. J. 70(2), 971-976 (1996).
    • (1996) Biophys. J. , vol.70 , Issue.2 , pp. 971-976
    • Strambini, G.B.1    Gabellieri, E.2
  • 75
    • 35748979712 scopus 로고    scopus 로고
    • Protein stability during freezing: Separation of stresses and mechanisms of protein stabilization
    • Bhatnagar BS, Bogner RH, Pikal MJ. Protein stability during freezing: separation of stresses and mechanisms of protein stabilization. Pharm. Dev. Technol. 12(5), 505-523 (2007).
    • (2007) Pharm. Dev. Technol. , vol.12 , Issue.5 , pp. 505-523
    • Bhatnagar, B.S.1    Bogner, R.H.2    Pikal, M.J.3
  • 76
    • 80054758768 scopus 로고    scopus 로고
    • Interactions of formulation excipients with proteins in solution and in the dried state
    • Ohtake S, Kita Y, Arakawa T. Interactions of formulation excipients with proteins in solution and in the dried state. Adv. Drug Deliv. Rev. 63(13), 1053-1073 (2011).
    • (2011) Adv. Drug Deliv. Rev. , vol.63 , Issue.13 , pp. 1053-1073
    • Ohtake, S.1    Kita, Y.2    Arakawa, T.3
  • 78
    • 0028902339 scopus 로고
    • Biopreservation. Putting proteins under glass
    • Fox K. Biopreservation. Putting proteins under glass. Science 267(5206), 1922-1923 (1995).
    • (1995) Science , vol.267 , Issue.5206 , pp. 1922-1923
    • Fox, K.1
  • 79
    • 0024549238 scopus 로고
    • An infrared spectroscopic study of the interactions of carbohydrates with dried proteins
    • Carpenter JF, Crowe JH. An infrared spectroscopic study of the interactions of carbohydrates with dried proteins. Biochemistry. 28(9), 3916-3922 (1989).
    • (1989) Biochemistry. , vol.28 , Issue.9 , pp. 3916-3922
    • Carpenter, J.F.1    Crowe, J.H.2
  • 80
    • 0027176042 scopus 로고
    • Separation of freezing-and drying-induced denaturation of lyophilized proteins using stress-specifc stabilization. II. Structural studies using infrared spectroscopy
    • Prestrelski SJ, Arakawa T, Carpenter JF. Separation of freezing-and drying-induced denaturation of lyophilized proteins using stress-specifc stabilization. II. Structural studies using infrared spectroscopy. Arch. Biochem. Biophys. 303(2), 465-473 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.303 , Issue.2 , pp. 465-473
    • Prestrelski, S.J.1    Arakawa, T.2    Carpenter, J.F.3
  • 81
    • 0028865701 scopus 로고
    • Optimization of lyophilization conditions for recombinant human interleukin-2 by dried-state conformational analysis using Fourier-transform infrared spectroscopy
    • Prestrelski SJ, Pikal KA, Arakawa T. Optimization of lyophilization conditions for recombinant human interleukin-2 by dried-state conformational analysis using Fourier-transform infrared spectroscopy. Pharm. Res. 12(9), 1250-1259 (1995).
    • (1995) Pharm. Res. , vol.12 , Issue.9 , pp. 1250-1259
    • Prestrelski, S.J.1    Pikal, K.A.2    Arakawa, T.3
  • 82
    • 0027272126 scopus 로고
    • Freeze-thaw studies of a model protein, lactate dehydrogenase, in the presence of cryoprotectants
    • Nema S, Avis KE. Freeze-thaw studies of a model protein, lactate dehydrogenase, in the presence of cryoprotectants. J. Parenter. Sci. Technol. 47(2), 76-83 (1993).
    • (1993) J. Parenter. Sci. Technol. , vol.47 , Issue.2 , pp. 76-83
    • Nema, S.1    Avis, K.E.2
  • 83
    • 0026350187 scopus 로고
    • Effect of formulation and freeze-drying on the long-term stability of rDNA-derived cytokines
    • Dawson PJ. Effect of formulation and freeze-drying on the long-term stability of rDNA-derived cytokines. Dev. Biol. Stand. 74, 273-282 (1992).
    • (1992) Dev. Biol. Stand. , vol.74 , pp. 273-282
    • Dawson, P.J.1
  • 84
    • 0030586740 scopus 로고    scopus 로고
    • Polymers protect lactate dehydrogenase during freeze-drying by inhibiting dissociation in the frozen state
    • Anchordoquy TJ, Carpenter JF. Polymers protect lactate dehydrogenase during freeze-drying by inhibiting dissociation in the frozen state. Arch. Biochem. Biophys. 332(2), 231-238 (1996).
    • (1996) Arch. Biochem. Biophys. , vol.332 , Issue.2 , pp. 231-238
    • Anchordoquy, T.J.1    Carpenter, J.F.2
  • 85
    • 0032190182 scopus 로고    scopus 로고
    • Effects of drying methods and additives on structure and function of actin: Mechanisms of dehydration-induced damage and its inhibition
    • Allison SD, Randolph TW, Manning MC, Middleton K, Davis A, Carpenter JF. Effects of drying methods and additives on structure and function of actin: mechanisms of dehydration-induced damage and its inhibition. Arch. Biochem. Biophys. 358(1), 171-181 (1998).
    • (1998) Arch. Biochem. Biophys. , vol.358 , Issue.1 , pp. 171-181
    • Allison, S.D.1    Randolph, T.W.2    Manning, M.C.3    Middleton, K.4    Davis, A.5    Carpenter, J.F.6
  • 87
    • 0032425839 scopus 로고    scopus 로고
    • Effects of additives on the stability of recombinant human factor XIII during freeze-drying and storage in the dried solid
    • Kreilgaard L, Frokjaer S, Flink JM, Randolph TW, Carpenter JF. Effects of additives on the stability of recombinant human factor XIII during freeze-drying and storage in the dried solid. Arch. Biochem. Biophys. 360(1), 121-134 (1998).
    • (1998) Arch. Biochem. Biophys. , vol.360 , Issue.1 , pp. 121-134
    • Kreilgaard, L.1    Frokjaer, S.2    Flink, J.M.3    Randolph, T.W.4    Carpenter, J.F.5
  • 88
    • 0029020745 scopus 로고
    • Increased stabilizing effects of amphiphilic excipients on freeze-drying of lactate dehydrogenase (LDH) by dispersion into sugar matrices
    • Izutsu K-I, Yoshioka S, Kojima S. Increased stabilizing effects of amphiphilic excipients on freeze-drying of lactate dehydrogenase (LDH) by dispersion into sugar matrices. Pharm. Res. 12(6), 838-843 (1995).
    • (1995) Pharm. Res. , vol.12 , Issue.6 , pp. 838-843
    • Izutsu, K.-I.1    Yoshioka, S.2    Kojima, S.3
  • 89
    • 0027256589 scopus 로고
    • Separation of freezing-and drying-induced denaturation of lyophilized proteins using stress-specifc stabilization: I. Enzyme activity and calorimetric studies
    • Carpenter JF, Prestrelski SJ, Arakawa T. Separation of freezing-and drying-induced denaturation of lyophilized proteins using stress-specifc stabilization: I. Enzyme activity and calorimetric studies. Arch. Biochem. Biophys. 303(2), 456-464 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.303 , Issue.2 , pp. 456-464
    • Carpenter, J.F.1    Prestrelski, S.J.2    Arakawa, T.3
  • 90
    • 78149311529 scopus 로고    scopus 로고
    • Investigation of PEG crystallization in frozen PEG-sucrose-water solutions: II. Characterization of the equilibrium behavior during freeze-thawing
    • Bhatnagar BS, Martin SM, Teagarden DL, Shalaev EY, Suryanarayanan R. Investigation of PEG crystallization in frozen PEG-sucrose-water solutions: II. Characterization of the equilibrium behavior during freeze-thawing. J. Pharm. Sci. 99 (11), 4510-4524 (2010).
    • (2010) J. Pharm. Sci. , vol.99 , Issue.11 , pp. 4510-4524
    • Bhatnagar, B.S.1    Martin, S.M.2    Teagarden, D.L.3    Shalaev, E.Y.4    Suryanarayanan, R.5
  • 92
    • 0030443567 scopus 로고    scopus 로고
    • Surface-induced denaturation of proteins during freezing and its inhibition by surfactants
    • Chang BS, Kendrick BS, Carpenter JF. Surface-induced denaturation of proteins during freezing and its inhibition by surfactants. J. Pharm. Sci. 85(12), 1325-1330 (1996).
    • (1996) J. Pharm. Sci. , vol.85 , Issue.12 , pp. 1325-1330
    • Chang, B.S.1    Kendrick, B.S.2    Carpenter, J.F.3
  • 93
    • 0027972452 scopus 로고
    • Feasibility study on spray-drying protein pharmaceuticals: Recombinant human growth hormone and tissue-type plasminogen activator
    • Mumenthaler M, Hsu CC, Pearlman R. Feasibility study on spray-drying protein pharmaceuticals: Recombinant human growth hormone and tissue-type plasminogen activator. Pharm. Res. 11(1), 12-20 (1994).
    • (1994) Pharm. Res. , vol.11 , Issue.1 , pp. 12-20
    • Mumenthaler, M.1    Hsu, C.C.2    Pearlman, R.3
  • 94
    • 0034671999 scopus 로고    scopus 로고
    • Protein denaturation during freezing and thawing in phosphate buffer systems: Monomeric and tetrameric β-galactosidase
    • Pikal-Cleland KA, Rodríguez-Hornedo N, Amidon GL, Carpenter JF. Protein denaturation during freezing and thawing in phosphate buffer systems: monomeric and tetrameric β-galactosidase. Arch. Biochem. Biophys. 384(2), 398-406 (2000).
    • (2000) Arch. Biochem. Biophys. , vol.384 , Issue.2 , pp. 398-406
    • Pikal-Cleland, K.A.1    Rodríguez-Hornedo, N.2    Amidon, G.L.3    Carpenter, J.F.4
  • 95
    • 0034833878 scopus 로고    scopus 로고
    • Lyophilization-induced protein denaturation in phosphate buffer systems: Monomeric and tetrameric beta-galactosidase
    • Pikal-Cleland KA, Carpenter JF. Lyophilization-induced protein denaturation in phosphate buffer systems: monomeric and tetrameric beta-galactosidase. J. Pharm. Sci. 90(9), 1255-1268 (2001).
    • (2001) J. Pharm. Sci. , vol.90 , Issue.9 , pp. 1255-1268
    • Pikal-Cleland, K.A.1    Carpenter, J.F.2
  • 96
    • 0036771258 scopus 로고    scopus 로고
    • Effect of glycine on pH changes and protein stability during freeze-thawing in phosphate buffer systems
    • Pikal-Cleland KA, Cleland JL, Anchordoquy TJ, Carpenter JF. Effect of glycine on pH changes and protein stability during freeze-thawing in phosphate buffer systems. J. Pharm. Sci. 91(9), 1969-1979 (2002).
    • (2002) J. Pharm. Sci. , vol.91 , Issue.9 , pp. 1969-1979
    • Pikal-Cleland, K.A.1    Cleland, J.L.2    Anchordoquy, T.J.3    Carpenter, J.F.4
  • 97
    • 33846140780 scopus 로고    scopus 로고
    • Antibody structure, instability, and formulation
    • Wang W, Singh S, Zeng DL, King K, Nema S. Antibody structure, instability, and formulation. J. Pharm. Sci. 96(1), 1-26 (2006).
    • (2006) J. Pharm. Sci. , vol.96 , Issue.1 , pp. 1-26
    • Wang, W.1    Singh, S.2    Zeng, D.L.3    King, K.4    Nema, S.5
  • 98
    • 0027729733 scopus 로고
    • The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation
    • Cleland JL, Powell MF, Shire SJ. The development of stable protein formulations: a close look at protein aggregation, deamidation, and oxidation. Crit. Rev. Ther. Drug Carrier Syst. 10(4), 307-377 (1993).
    • (1993) Crit. Rev. Ther. Drug Carrier Syst. , vol.10 , Issue.4 , pp. 307-377
    • Cleland, J.L.1    Powell, M.F.2    Shire, S.J.3
  • 99
    • 33747488943 scopus 로고    scopus 로고
    • Formulation and delivery issues for monoclonal antibody therapeutics
    • Daugherty AL, Mrsny RJ. Formulation and delivery issues for monoclonal antibody therapeutics. Adv. Drug Deliv. Rev. 58(5-6), 686-706 (2006).
    • (2006) Adv. Drug Deliv. Rev. , vol.58 , Issue.5-6 , pp. 686-706
    • Daugherty, A.L.1    Mrsny, R.J.2
  • 100
    • 23844447975 scopus 로고    scopus 로고
    • Mechanism of protein stabilization by sugars during freeze-drying and storage: Native structure preservation, specifc interaction, and/or immobilization in a glassy matrix?
    • Chang LL, Shepherd D, Sun J et al. Mechanism of protein stabilization by sugars during freeze-drying and storage: native structure preservation, specifc interaction, and/or immobilization in a glassy matrix? J. Pharm. Sci. 94(7), 1427-1444 (2005).
    • (2005) J. Pharm. Sci. , vol.94 , Issue.7 , pp. 1427-1444
    • Chang, L.L.1    Shepherd, D.2    Sun, J.3
  • 102
    • 34548034190 scopus 로고    scopus 로고
    • The challenge of drying method selection for protein pharmaceuticals: Product quality implications
    • Abdul-Fattah AM, Kalonia DS, Pikal MJ. The challenge of drying method selection for protein pharmaceuticals: product quality implications. J. Pharm. Sci. 96 (8), 1886-1916 (2007).
    • (2007) J. Pharm. Sci. , vol.96 , Issue.8 , pp. 1886-1916
    • Abdul-Fattah, A.M.1    Kalonia, D.S.2    Pikal, M.J.3
  • 103
    • 0141798534 scopus 로고    scopus 로고
    • Statistical modeling of protein spray drying at the lab scale
    • Prinn K, Constantino HR, Tracy M. Statistical modeling of protein spray drying at the lab scale. AAPS PharmSciTech. 3(1) (2002).
    • (2002) AAPS PharmSciTech. , vol.3 , Issue.1
    • Prinn, K.1    Constantino, H.R.2    Tracy, M.3
  • 104
    • 0037148657 scopus 로고    scopus 로고
    • The effect of process variables on the degradation and physical properties of spray dried insulin intended for inhalation
    • Ståhl K, Claesson M, Lilliehorn P, Linden H, Backstrom K. The effect of process variables on the degradation and physical properties of spray dried insulin intended for inhalation. Int. J. Pharm. 233, 227-237 (2002).
    • (2002) Int. J. Pharm. , vol.233 , pp. 227-237
    • Ståhl, K.1    Claesson, M.2    Lilliehorn, P.3    Linden, H.4    Backstrom, K.5
  • 106
    • 38349150992 scopus 로고    scopus 로고
    • The impact of drying method and formulation on the physical properties and stability of methionyl human growth hormone in the amorphous solid state
    • Abdul-Fattah AM, Lechuga-Ballesteros D, Kalonia DS, Pikal MJ. The impact of drying method and formulation on the physical properties and stability of methionyl human growth hormone in the amorphous solid state. J. Pharm. Sci. 97(1), 163-184 (2008).
    • (2008) J. Pharm. Sci. , vol.97 , Issue.1 , pp. 163-184
    • Abdul-Fattah, A.M.1    Lechuga-Ballesteros, D.2    Kalonia, D.S.3    Pikal, M.J.4
  • 108
    • 0031793406 scopus 로고    scopus 로고
    • Effect of mannitol crystallization on the stability and aerosol performance of a spray-dried pharmaceutical protein, recombinant humanized anti-IgE monoclonal antibody
    • Costantino HR, Andya JD, Nguyen PA et al. Effect of mannitol crystallization on the stability and aerosol performance of a spray-dried pharmaceutical protein, recombinant humanized anti-IgE monoclonal antibody. J. Pharm. Sci. 87(11), 1406-1411 (1998).
    • (1998) J. Pharm. Sci. , vol.87 , Issue.11 , pp. 1406-1411
    • Costantino, H.R.1    Andya, J.D.2    Nguyen, P.A.3
  • 109
    • 84875407167 scopus 로고    scopus 로고
    • The infuence of lysozyme on mannitol polymorphism in freeze-dried and spray-dried formulations depends on the selection of the drying process
    • Grohganz H, Lee Y-Y, Rantanen J, Yang M. The infuence of lysozyme on mannitol polymorphism in freeze-dried and spray-dried formulations depends on the selection of the drying process. Int. J. Pharm. 447(1-2), 224-230 (2013).
    • (2013) Int. J. Pharm. , vol.447 , Issue.1-2 , pp. 224-230
    • Grohganz, H.1    Lee, Y.-Y.2    Rantanen, J.3    Yang, M.4
  • 110
    • 25444466477 scopus 로고    scopus 로고
    • Thermodynamic and dynamic factors involved in the stability of native protein structure in amorphous solids in relation to levels of hydration
    • Hill JJ, Shalaev EY, Zograf G. Thermodynamic and dynamic factors involved in the stability of native protein structure in amorphous solids in relation to levels of hydration. J. Pharm. Sci. 94 (8), 1636-1667 (2005).
    • (2005) J. Pharm. Sci. , vol.94 , Issue.8 , pp. 1636-1667
    • Hill, J.J.1    Shalaev, E.Y.2    Zograf, G.3
  • 111
    • 12344290280 scopus 로고    scopus 로고
    • Spray-drying of proteins: Effects of sorbitol and trehalose on aggregation and FT-IR amide i spectrum of an immunoglobulin
    • Maury M, Murphy K, Kumar S, Mauerer A, Lee G. Spray-drying of proteins: effects of sorbitol and trehalose on aggregation and FT-IR amide I spectrum of an immunoglobulin. G Eur. J. Pharm. Biopharm. 59(2), 251-261 (2005).
    • (2005) G Eur. J. Pharm. Biopharm. , vol.59 , Issue.2 , pp. 251-261
    • Maury, M.1    Murphy, K.2    Kumar, S.3    Mauerer, A.4    Lee, G.5
  • 112
    • 0036909494 scopus 로고    scopus 로고
    • Effect of sucrose and trehalose on the preservation of the native structure of spray-dried lysozyme
    • Liao Y-H, Brown MB, Nazir T, Quader A, Martin GP. Effect of sucrose and trehalose on the preservation of the native structure of spray-dried lysozyme. Pharm. Res. 19 (12), 1847-1853 (2002).
    • (2002) Pharm. Res. , vol.19 , Issue.12 , pp. 1847-1853
    • Liao, Y.-H.1    Brown, M.B.2    Nazir, T.3    Quader, A.4    Martin, G.P.5
  • 113
    • 84873706384 scopus 로고    scopus 로고
    • The effect of amino acid excipients on morphology and solid-state properties of multi-component spray-dried formulations for pulmonary delivery of biomacromolecules
    • Sou T, Kaminskas LM, Nguyen T-H, Carlberg R, McIntosh MP, Morton DA. The effect of amino acid excipients on morphology and solid-state properties of multi-component spray-dried formulations for pulmonary delivery of biomacromolecules. Eur. J. Pharm. Biopharm. 83, 234-243 (2012).
    • (2012) Eur. J. Pharm. Biopharm. , vol.83 , pp. 234-243
    • Sou, T.1    Kaminskas, L.M.2    Nguyen, T.-H.3    Carlberg, R.4    McIntosh, M.P.5    Morton, D.A.6
  • 114
    • 33947287573 scopus 로고    scopus 로고
    • Drying-induced variations in physico-chemical properties of amorphous pharmaceuticals and their impact on stability (I): Stability of a monoclonal antibody
    • Abdul-Fattah AM, Truong-le VU, Yee L et al. Drying-induced variations in physico-chemical properties of amorphous pharmaceuticals and their impact on stability (I): stability of a monoclonal antibody. J. Pharm. Sci. 96(8), 1983-2008 (2008).
    • (2008) J. Pharm. Sci. , vol.96 , Issue.8 , pp. 1983-2008
    • Abdul-Fattah, A.M.1    Truong-Le, V.U.2    Yee, L.3
  • 115
    • 33745027645 scopus 로고    scopus 로고
    • Dry powder aerosol drug delivery-Opportunities for colloid and surface scientists
    • Chan HK. Dry powder aerosol drug delivery-Opportunities for colloid and surface scientists. Colloids Surf. A Physicochem. Eng. Asp. 284-285, 50-55 (2006).
    • (2006) Colloids Surf. A Physicochem. Eng. Asp. , vol.284-285 , pp. 50-55
    • Chan, H.K.1
  • 116
    • 33750804217 scopus 로고    scopus 로고
    • Particle engineering techniques for inhaled biopharmaceuticals
    • Shoyele S a, Cawthorne S. Particle engineering techniques for inhaled biopharmaceuticals. Adv. Drug Deliv. Rev. 58(9-10), 1009-1029 (2006).
    • (2006) Adv. Drug Deliv. Rev. , vol.58 , Issue.9-10 , pp. 1009-1029
    • Shoyele, S.A.1    Cawthorne, S.2
  • 117
    • 79151477339 scopus 로고    scopus 로고
    • Particle engineering of materials for oral inhalation by dry powder inhalers. I-Particles of sugar excipients (trehalose and raffnose) for protein delivery
    • Ogáin ON, Li J, Tajber L, Corrigan OI, Healy AM. Particle engineering of materials for oral inhalation by dry powder inhalers. I-Particles of sugar excipients (trehalose and raffnose) for protein delivery. Int. J. Pharm. 405(1-2), 23-35 (2011).
    • (2011) Int. J. Pharm. , vol.405 , Issue.1-2 , pp. 23-35
    • Ogáin, O.N.1    Li, J.2    Tajber, L.3    Corrigan, O.I.4    Healy, A.M.5
  • 118
    • 4644330189 scopus 로고    scopus 로고
    • Aerosolization properties, surface composition and physical state of spray-dried protein powders
    • Bosquillon C, Rouxhet PG, Ahimou F et al. Aerosolization properties, surface composition and physical state of spray-dried protein powders. J. Control. Release 99(3), 357-367 (2004).
    • (2004) J. Control. Release , vol.99 , Issue.3 , pp. 357-367
    • Bosquillon, C.1    Rouxhet, P.G.2    Ahimou, F.3
  • 119
    • 31144432665 scopus 로고    scopus 로고
    • EXUBERA: Pharmaceutical development of a novel product for pulmonary delivery of insulin
    • White S, Bennett DB, Cheu S et al. EXUBERA: pharmaceutical development of a novel product for pulmonary delivery of insulin. Diabetes Technol. Ther. 7(6), 896-906 (2005).
    • (2005) Diabetes Technol. Ther. , vol.7 , Issue.6 , pp. 896-906
    • White, S.1    Bennett, D.B.2    Cheu, S.3
  • 120
    • 77952503692 scopus 로고    scopus 로고
    • The failure of exubera: Are we beating a dead horse?
    • Heinemann L. The failure of exubera: are we beating a dead horse? J. Diabetes Sci. Technol. 2(3), 518-29 ( 2008).
    • (2008) J. Diabetes Sci. Technol. , vol.2 , Issue.3 , pp. 518-529
    • Heinemann, L.1
  • 122
    • 34748867725 scopus 로고    scopus 로고
    • Novel approaches in microparticulate PLGA delivery systems encapsulating proteins
    • Taluja A, Youn YS, Bae YH. Novel approaches in microparticulate PLGA delivery systems encapsulating proteins. J. Mater. Chem. 17(38), 4002 (2007).
    • (2007) J. Mater. Chem. , vol.17 , Issue.38 , pp. 4002
    • Taluja, A.1    Youn, Y.S.2    Bae, Y.H.3
  • 123
    • 58149152977 scopus 로고    scopus 로고
    • Development of protein delivery microsphere system by a novel s/o/o/w multi-emulsion
    • Yuan W, Wu F, Guo M, Jin T. Development of protein delivery microsphere system by a novel s/o/o/w multi-emulsion. Eur. J. Pharm. Sci. 36, 212-218 (2009).
    • (2009) Eur. J. Pharm. Sci. , vol.36 , pp. 212-218
    • Yuan, W.1    Wu, F.2    Guo, M.3    Jin, T.4
  • 124
    • 4544227115 scopus 로고    scopus 로고
    • Microparticle formation and its mechanism in single and double emulsion solvent evaporation
    • Rosca ID, Watari F, Uo M. Microparticle formation and its mechanism in single and double emulsion solvent evaporation. J. Control. Release 99(2), 271-280 (2004).
    • (2004) J. Control. Release , vol.99 , Issue.2 , pp. 271-280
    • Rosca, I.D.1    Watari, F.2    Uo, M.3
  • 125
    • 79955830518 scopus 로고    scopus 로고
    • The manufacturing techniques of drug-loaded polymeric nanoparticles from preformed polymers
    • Grabnar PA, Kristl J. The manufacturing techniques of drug-loaded polymeric nanoparticles from preformed polymers. J. Microencapsul. 28(4), 323-35 (2011).
    • (2011) J. Microencapsul. , vol.28 , Issue.4 , pp. 323-335
    • Grabnar, P.A.1    Kristl, J.2
  • 127
    • 0038445582 scopus 로고    scopus 로고
    • Biodegradable microspheres for protein delivery
    • Sinha VR, Trehan A. Biodegradable microspheres for protein delivery J. Control. Release 90(3), 261-280 (2003).
    • (2003) J. Control. Release , vol.90 , Issue.3 , pp. 261-280
    • Sinha, V.R.1    Trehan, A.2
  • 128
    • 57849131157 scopus 로고    scopus 로고
    • Preparation of alginate coated chitosan microparticles for vaccine delivery
    • Li X, Kong X, Shi S et al. Preparation of alginate coated chitosan microparticles for vaccine delivery BMC Biotechnol. 8(89) (2008).
    • (2008) BMC Biotechnol. , vol.8 , Issue.89
    • Li, X.1    Kong, X.2    Shi, S.3
  • 129
    • 84893314042 scopus 로고    scopus 로고
    • Pullulan-based nano particles: Future therapeutic applications in transmucosal protein delivery
    • Grenha A, Rodrigues S. Pullulan-based nano particles: future therapeutic applications in transmucosal protein delivery Ther. Deliv. 4(11), 1339-1341 (2013).
    • (2013) Ther. Deliv. , vol.4 , Issue.11 , pp. 1339-1341
    • Grenha, A.1    Rodrigues, S.2
  • 130
    • 19444373936 scopus 로고    scopus 로고
    • Development of a novel sustained release formulation of recombinant human growth hormone using sodium hyaluronate microparticles
    • Kim S, Hahn S, Kim M, Kim D, Lee Y. Development of a novel sustained release formulation of recombinant human growth hormone using sodium hyaluronate microparticles. J. Control. Release. 104(2), 323-335 (2005).
    • (2005) J. Control. Release. , vol.104 , Issue.2 , pp. 323-335
    • Kim, S.1    Hahn, S.2    Kim, M.3    Kim, D.4    Lee, Y.5
  • 131
    • 33947240316 scopus 로고    scopus 로고
    • Protein complexed with chondroitin sulfate in poly(lactide-co-glycolide) microspheres
    • Lee ES, Park K-H, Kang D et al. Protein complexed with chondroitin sulfate in poly(lactide-co-glycolide) microspheres. Biomaterials 28(17), 2754-2762 (2007).
    • (2007) Biomaterials , vol.28 , Issue.17 , pp. 2754-2762
    • Lee, E.S.1    Park, K.-H.2    Kang, D.3
  • 132
    • 84877289497 scopus 로고    scopus 로고
    • An overview of preparation and evaluation sustained-release injectable microspheres
    • Hu L, Zhang H, Song W An overview of preparation and evaluation sustained-release injectable microspheres. J. Microencapsul. 30(4), 369-382 (2013).
    • (2013) J. Microencapsul. , vol.30 , Issue.4 , pp. 369-382
    • Hu, L.1    Zhang, H.2    Song, W.3
  • 133
    • 84865314548 scopus 로고    scopus 로고
    • Recent advances in polymeric microspheres for parenteral drug delivery-part 1
    • Mao S, Guo C, Shi Y, Li LC. Recent advances in polymeric microspheres for parenteral drug delivery-part 1. Expert Opin. Drug Deliv. 9(9), 1161-1176 (2012).
    • (2012) Expert Opin. Drug Deliv. , vol.9 , Issue.9 , pp. 1161-1176
    • Mao, S.1    Guo, C.2    Shi, Y.3    Li, L.C.4
  • 134
    • 65949087875 scopus 로고    scopus 로고
    • A novel approach to prepare insulin-loaded poly(lactic-co-glycolic acid) microcapsules and the protein stability study
    • Emami J, Hamishehkar H, Najafabadi AR et al. A novel approach to prepare insulin-loaded poly(lactic-co-glycolic acid) microcapsules and the protein stability study J. Pharm. Sci. 98(5), 1712-1731 (2009).
    • (2009) J. Pharm. Sci. , vol.98 , Issue.5 , pp. 1712-1731
    • Emami, J.1    Hamishehkar, H.2    Najafabadi, A.R.3
  • 135
    • 77955439513 scopus 로고    scopus 로고
    • Controlled release of bioactive recombinant human growth hormone from PLGA microparticles
    • Raf M, Singh SM, Kanchan V, Anish CK, Panda AK. Controlled release of bioactive recombinant human growth hormone from PLGA microparticles. J. Microencapsul. 27(6), 552-560 (2010).
    • (2010) J. Microencapsul. , vol.27 , Issue.6 , pp. 552-560
    • Raf, M.1    Singh, S.M.2    Kanchan, V.3    Anish, C.K.4    Panda, A.K.5
  • 136
    • 14844317382 scopus 로고    scopus 로고
    • Strategic approaches for overcoming peptide and protein instability within biodegradable nano-and microparticles
    • Bilati U, Allémann E, Doelker E. Strategic approaches for overcoming peptide and protein instability within biodegradable nano-and microparticles. Eur. J. Pharm. Biopharm. 59(3), 375-388 (2005).
    • (2005) Eur. J. Pharm. Biopharm. , vol.59 , Issue.3 , pp. 375-388
    • Bilati, U.1    Allémann, E.2    Doelker, E.3
  • 137
    • 84880836617 scopus 로고    scopus 로고
    • Developing long-acting growth hormone formulations
    • Cawley P, Wilkinson I, Ross RJ. Developing long-acting growth hormone formulations. Clin. Endocrinol. (Oxf). 79(3), 305-309 (2013).
    • (2013) Clin. Endocrinol. (Oxf). , vol.79 , Issue.3 , pp. 305-309
    • Cawley, P.1    Wilkinson, I.2    Ross, R.J.3
  • 138
    • 0343907187 scopus 로고    scopus 로고
    • One-and three-month release injectable microspheres of the LH-RH superagonist leuprorelin acetate
    • Okada H. One-and three-month release injectable microspheres of the LH-RH superagonist leuprorelin acetate. Adv. Drug Deliv. Rev. 28(1), 43-70 (1997).
    • (1997) Adv. Drug Deliv. Rev. , vol.28 , Issue.1 , pp. 43-70
    • Okada, H.1
  • 139
    • 0017536083 scopus 로고
    • Degradation rates of oral resorbable implants (polylactates and polyglycolates): Rate modifcation with changes in PLA/PGA copolymer ratios
    • Miller RA, Brady JM, Cutright DE. Degradation rates of oral resorbable implants (polylactates and polyglycolates): rate modifcation with changes in PLA/PGA copolymer ratios. J. Biomed. Mater. Res. 11(5), 711-719 (1977).
    • (1977) J. Biomed. Mater. Res. , vol.11 , Issue.5 , pp. 711-719
    • Miller, R.A.1    Brady, J.M.2    Cutright, D.E.3
  • 141
    • 0036752497 scopus 로고    scopus 로고
    • Enzyme-carrying polymeric nanofbers prepared via electrospinning for use as unique biocatalysts
    • Jia H, Zhu G, Vugrinovich B, Kataphinan W, Reneker DH, Wang P. Enzyme-carrying polymeric nanofbers prepared via electrospinning for use as unique biocatalysts. Biotechnol. Prog. 18(5), 1027-1032 (2002).
    • (2002) Biotechnol. Prog. , vol.18 , Issue.5 , pp. 1027-1032
    • Jia, H.1    Zhu, G.2    Vugrinovich, B.3    Kataphinan, W.4    Reneker, D.H.5    Wang, P.6
  • 142
    • 27744591467 scopus 로고    scopus 로고
    • A facile technique to prepare biodegradable coaxial electrospun nanofbers for controlled release of bioactive agents
    • Jiang H, Hu Y, Li Y, Zhao P, Zhu K, Chen W. A facile technique to prepare biodegradable coaxial electrospun nanofbers for controlled release of bioactive agents. J. Control. Release 108(2-3), 237-243 (2005).
    • (2005) J. Control. Release , vol.108 , Issue.2-3 , pp. 237-243
    • Jiang, H.1    Hu, Y.2    Li, Y.3    Zhao, P.4    Zhu, K.5    Chen, W.6
  • 143
    • 47049128960 scopus 로고    scopus 로고
    • Structural stability and release profles of proteins from core-shell poly (DL-lactide) ultrafne fbers prepared by emulsion electrospinning
    • Yang Y, Li X, Cui W, Zhou S, Tan R, Wang C. Structural stability and release profles of proteins from core-shell poly (DL-lactide) ultrafne fbers prepared by emulsion electrospinning. J. Biomed. Mater. Res. A. 86(2), 374-385 (2008).
    • (2008) J. Biomed. Mater. Res. A. , vol.86 , Issue.2 , pp. 374-385
    • Yang, Y.1    Li, X.2    Cui, W.3    Zhou, S.4    Tan, R.5    Wang, C.6
  • 144
  • 145
    • 79953058363 scopus 로고    scopus 로고
    • Sustained release of VEGF by coaxial electrospun dextran/PLGA fbrous membranes in vascular tissue engineering
    • Jia X, Zhao C, Li P et al. Sustained release of VEGF by coaxial electrospun dextran/PLGA fbrous membranes in vascular tissue engineering. J. Biomater. Sci. Polym. Ed. 22(13), 1811-1827 (2011).
    • (2011) J. Biomater. Sci. Polym. Ed. , vol.22 , Issue.13 , pp. 1811-1827
    • Jia, X.1    Zhao, C.2    Li, P.3
  • 147
    • 79251642233 scopus 로고    scopus 로고
    • N-Dodecyl-β-D-maltoside inhibits aggregation of human interferon-β-1b and reduces its immunogenicity
    • Rifkin RA, Maggio ET, Dike S, Kerr DA, Levy M. n-Dodecyl-β-D-maltoside inhibits aggregation of human interferon-β-1b and reduces its immunogenicity. J. Neuroimmune Pharmacol. 6(1), 158-162 (2011).
    • (2011) J. Neuroimmune Pharmacol. , vol.6 , Issue.1 , pp. 158-162
    • Rifkin, R.A.1    Maggio, E.T.2    Dike, S.3    Kerr, D.A.4    Levy, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.