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Volumn 260, Issue 1, 2003, Pages 149-156

Conformational stability of a model protein (bovine serum albumin) during primary emulsification process of PLGA microspheres synthesis

Author keywords

BSA; Conformational stability; Differential scanning calorimetry; Emulsification; Poly(D,L lactide co glycolide); Protein

Indexed keywords

2 HYDROXYPROPYL BETA CYCLODEXTRIN; BOVINE SERUM ALBUMIN; DODECYL SULFATE SODIUM; EXCIPIENT; MANNITOL; MICROSPHERE; POLYGLACTIN;

EID: 0038344725     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-5173(03)00263-1     Document Type: Article
Times cited : (64)

References (30)
  • 1
    • 0031933272 scopus 로고    scopus 로고
    • Solvent evaporation processes for the production of controlled release biodegradable microsphere formulations for therapeutics and vaccines
    • Cleland J.L. Solvent evaporation processes for the production of controlled release biodegradable microsphere formulations for therapeutics and vaccines. Biotechnol. Prog. 14:1998;102-107.
    • (1998) Biotechnol. Prog. , vol.14 , pp. 102-107
    • Cleland, J.L.1
  • 2
    • 0029859532 scopus 로고    scopus 로고
    • Stable formulations of recombinant human growth hormone and interferon-gamma for microencapsulation in biodegradable microspheres
    • Cleland J.L., Jones A.J. Stable formulations of recombinant human growth hormone and interferon-gamma for microencapsulation in biodegradable microspheres. Pharm. Res. 13:1996;1464-1475.
    • (1996) Pharm. Res. , vol.13 , pp. 1464-1475
    • Cleland, J.L.1    Jones, A.J.2
  • 3
    • 0025731293 scopus 로고
    • Controlled delivery systems for proteins based on poly(lactic/glycolic acid) microspheres
    • Cohen S., Yoshioka T., Lucarelli M., Hwang L.H., Langer R. Controlled delivery systems for proteins based on poly(lactic/glycolic acid) microspheres. Pharm. Res. 8:1991;713-720.
    • (1991) Pharm. Res. , vol.8 , pp. 713-720
    • Cohen, S.1    Yoshioka, T.2    Lucarelli, M.3    Hwang, L.H.4    Langer, R.5
  • 4
    • 0031752709 scopus 로고    scopus 로고
    • Protein delivery from poly(lactic-co-glycolic acid) biodegradable microspheres: Release kinetics and stability issues
    • Crotts G., Park T.G. Protein delivery from poly(lactic-co-glycolic acid) biodegradable microspheres: release kinetics and stability issues. J. Microencapsul. 15:1998;699-713.
    • (1998) J. Microencapsul. , vol.15 , pp. 699-713
    • Crotts, G.1    Park, T.G.2
  • 5
    • 0013893808 scopus 로고
    • The interaction of bovine plasma albumin with detergent anions. Stoichiometry and mechanism of binding of alkylbenzenesulfonates
    • Decker R.V., Foster J.F. The interaction of bovine plasma albumin with detergent anions. Stoichiometry and mechanism of binding of alkylbenzenesulfonates. Biochemistry. 5:1966;1242-1254.
    • (1966) Biochemistry , vol.5 , pp. 1242-1254
    • Decker, R.V.1    Foster, J.F.2
  • 6
    • 0030979596 scopus 로고    scopus 로고
    • DSC studies on bovine serum albumin denaturation. Effects of ionic strength and SDS concentration
    • Giancola C., De Sena C., Fessas D., Graciano G., Barone G. DSC studies on bovine serum albumin denaturation. Effects of ionic strength and SDS concentration. Int. J. Biol. Macromol. 20:1997;193-204.
    • (1997) Int. J. Biol. Macromol. , vol.20 , pp. 193-204
    • Giancola, C.1    De Sena, C.2    Fessas, D.3    Graciano, G.4    Barone, G.5
  • 7
    • 0030828875 scopus 로고    scopus 로고
    • Chronic local tissue reactions, long-term immunogenicity and immunologic priming of mice and guinea pigs to tetanus toxoid encapsulated in biodegradable polymer microspheres composed of poly lactide-co-glycolide polymers
    • Gupta R.K., Alroy J., Alonso M.J., Langer R., Siber G.R. Chronic local tissue reactions, long-term immunogenicity and immunologic priming of mice and guinea pigs to tetanus toxoid encapsulated in biodegradable polymer microspheres composed of poly lactide-co-glycolide polymers. Vaccine. 15:1997;1716-1723.
    • (1997) Vaccine , vol.15 , pp. 1716-1723
    • Gupta, R.K.1    Alroy, J.2    Alonso, M.J.3    Langer, R.4    Siber, G.R.5
  • 8
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He X.M., Carter D.C. Atomic structure and chemistry of human serum albumin. Nature. 358:1992;209-215.
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 9
    • 0027409962 scopus 로고
    • The preparation and characterization of poly(lactide-co-glycolide) microparticles. II. The entrapment of a model protein using a (water-in-oil)-in-water emulsion solvent evaporation technique
    • Jeffery H., Davis S.S., O'Hagan D.T. The preparation and characterization of poly(lactide-co-glycolide) microparticles. II. The entrapment of a model protein using a (water-in-oil)-in-water emulsion solvent evaporation technique. Pharm. Res. 10:1993;362-368.
    • (1993) Pharm. Res. , vol.10 , pp. 362-368
    • Jeffery, H.1    Davis, S.S.2    O'Hagan, D.T.3
  • 10
    • 0037133127 scopus 로고    scopus 로고
    • Assessment of protein release kinetic, stability and protein polymer interaction of lysozyme encapsulated poly(D,L-lactide-co-glycolide) microspheres
    • Jiang G., Woo B.H., Kang F., Singh J., DeLuca P.P. Assessment of protein release kinetic, stability and protein polymer interaction of lysozyme encapsulated poly(D,L-lactide-co-glycolide) microspheres. J. Control. Release. 79:2002;137-145.
    • (2002) J. Control. Release , vol.79 , pp. 137-145
    • Jiang, G.1    Woo, B.H.2    Kang, F.3    Singh, J.4    DeLuca, P.P.5
  • 11
    • 0036001394 scopus 로고    scopus 로고
    • Lysozyme stability in primary emulsification for PLGA microsphere preparation: Effect of recovery methods and stabilizing excipients
    • Kang F., Jiang G., Hinderliter A., DeLuca P.P., Singh J. Lysozyme stability in primary emulsification for PLGA microsphere preparation: effect of recovery methods and stabilizing excipients. Pharm. Res. 19:2002;629-633.
    • (2002) Pharm. Res. , vol.19 , pp. 629-633
    • Kang, F.1    Jiang, G.2    Hinderliter, A.3    DeLuca, P.P.4    Singh, J.5
  • 12
    • 0001719160 scopus 로고    scopus 로고
    • Microencapsulation of human growth hormone within biodegradable polyester microspheres: Protein aggregation stability and incomplete release mechanism
    • Kim H.K., Park T.G. Microencapsulation of human growth hormone within biodegradable polyester microspheres: protein aggregation stability and incomplete release mechanism. Biotechnol. Bioeng. 65:1999;659-667.
    • (1999) Biotechnol. Bioeng. , vol.65 , pp. 659-667
    • Kim, H.K.1    Park, T.G.2
  • 13
    • 0034665495 scopus 로고    scopus 로고
    • Inactivation of lysozyme by sonication under conditions relevant to microencapsulation
    • Krishnamurthy R., Lumpkin J.A., Sridhar R. Inactivation of lysozyme by sonication under conditions relevant to microencapsulation. Int. J. Pharm. 205:2000;23-34.
    • (2000) Int. J. Pharm. , vol.205 , pp. 23-34
    • Krishnamurthy, R.1    Lumpkin, J.A.2    Sridhar, R.3
  • 14
    • 0035663205 scopus 로고    scopus 로고
    • In situ study of insulin aggregation induced by water-organic solvent interface
    • Kwon Y.M., Baudys M., Knutson K., Kim S.W. In situ study of insulin aggregation induced by water-organic solvent interface. Pharm. Res. 18:2001;1754-1759.
    • (2001) Pharm. Res. , vol.18 , pp. 1754-1759
    • Kwon, Y.M.1    Baudys, M.2    Knutson, K.3    Kim, S.W.4
  • 15
    • 0030968040 scopus 로고    scopus 로고
    • Spectroscopic characterization of the inclusion complex of a luteinizing hormone-releasing hormone agonist, buserelin acetate, with dimethyl-β-cyclodextrin
    • Matsubara K., Irie T., Uekama K. Spectroscopic characterization of the inclusion complex of a luteinizing hormone-releasing hormone agonist, buserelin acetate, with dimethyl-β-cyclodextrin. Chem. Pharm. Bull. 45:1997;378-383.
    • (1997) Chem. Pharm. Bull. , vol.45 , pp. 378-383
    • Matsubara, K.1    Irie, T.2    Uekama, K.3
  • 16
    • 0031398790 scopus 로고    scopus 로고
    • Microencapsulation of rh-erythropoietin using biodegradable poly(D,L-lactide-co-glycolide): Protein stability and the effects of stabilizing excipients
    • Morlock M., Koll H., Winter G., Kissel T. Microencapsulation of rh-erythropoietin using biodegradable poly(D,L-lactide-co-glycolide): protein stability and the effects of stabilizing excipients. Eur. J. Pharm. Biopharm. 43:1997;29-36.
    • (1997) Eur. J. Pharm. Biopharm. , vol.43 , pp. 29-36
    • Morlock, M.1    Koll, H.2    Winter, G.3    Kissel, T.4
  • 17
    • 0032484233 scopus 로고    scopus 로고
    • Erythropoietin loaded microspheres prepared from biodegradable LPLG-PEO-LPLG triblock copolymers: Protein stabilization and in vitro release properties
    • Morlock M., Kissel T., Li Y.X., Koll H., Winter G. Erythropoietin loaded microspheres prepared from biodegradable LPLG-PEO-LPLG triblock copolymers: protein stabilization and in vitro release properties. J. Control. Release. 56:1998;105-115.
    • (1998) J. Control. Release , vol.56 , pp. 105-115
    • Morlock, M.1    Kissel, T.2    Li, Y.X.3    Koll, H.4    Winter, G.5
  • 18
    • 0345084475 scopus 로고    scopus 로고
    • A new preparation method for protein loaded poly(D,L-lactic-co-glycolic acid) microspheres and protein release mechanism study
    • Park T.G., Lee H.Y., Nam Y.S. A new preparation method for protein loaded poly(D,L-lactic-co-glycolic acid) microspheres and protein release mechanism study. J. Control. Release. 55:1998;181-191.
    • (1998) J. Control. Release , vol.55 , pp. 181-191
    • Park, T.G.1    Lee, H.Y.2    Nam, Y.S.3
  • 19
    • 0033956125 scopus 로고    scopus 로고
    • Conformational issues in the characterization of proteins
    • Price N.C. Conformational issues in the characterization of proteins. Biotechnol. Appl. Biochem. 31:2000;29-40.
    • (2000) Biotechnol. Appl. Biochem. , vol.31 , pp. 29-40
    • Price, N.C.1
  • 20
    • 14444277713 scopus 로고    scopus 로고
    • Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry
    • Remmele R.L., Nightlinger N.S., Srinivasan S., Gombotz W.R. Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry. Pharm. Res. 15:1998;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
  • 21
    • 0032723478 scopus 로고    scopus 로고
    • Protein behavior at the water/methylene chloride interface
    • Sah H. Protein behavior at the water/methylene chloride interface. J. Pharm. Sci. 88:1999a;1320-1325.
    • (1999) J. Pharm. Sci. , vol.88 , pp. 1320-1325
    • Sah, H.1
  • 22
    • 0033039914 scopus 로고    scopus 로고
    • Stabilization of proteins against methylene chloride/water interface-induced denaturation and aggregation
    • Sah H. Stabilization of proteins against methylene chloride/water interface-induced denaturation and aggregation. J. Control. Release. 58:1999b;143-151.
    • (1999) J. Control. Release , vol.58 , pp. 143-151
    • Sah, H.1
  • 24
  • 26
    • 0033635054 scopus 로고    scopus 로고
    • Protein instability in poly(lactic-co-glycolic acid) microparticles
    • van de Weert M., Hennink W.E., Jiskoot W. Protein instability in poly(lactic-co-glycolic acid) microparticles. Pharm. Res. 17:2000a;1159-1167.
    • (2000) Pharm. Res. , vol.17 , pp. 1159-1167
    • Van De Weert, M.1    Hennink, W.E.2    Jiskoot, W.3
  • 27
    • 0034601661 scopus 로고    scopus 로고
    • The effect of a water/organic solvent interface on the structural stability of lysozyme
    • van de Weert M., Hoechstetter J., Hennink W.E., Crommelin D.J. The effect of a water/organic solvent interface on the structural stability of lysozyme. J. Control. Release. 68:2000b;351-359.
    • (2000) J. Control. Release , vol.68 , pp. 351-359
    • Van De Weert, M.1    Hoechstetter, J.2    Hennink, W.E.3    Crommelin, D.J.4
  • 28
    • 0025046965 scopus 로고
    • Differential scanning calorimetric studies on bovine serum albumin. I. Effects of pH and ionic strength
    • Yamasaki M., Yano H., Auki K. Differential scanning calorimetric studies on bovine serum albumin. I. Effects of pH and ionic strength. Int. J. Biol. Macromol. 12:1990;263-268.
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 263-268
    • Yamasaki, M.1    Yano, H.2    Auki, K.3
  • 29
    • 0030465765 scopus 로고    scopus 로고
    • Differential scanning calorimetric studies on bovine serum albumin. IV. Effect of anionic surfactants with various lengths of hydrocarbon chain
    • Yamasaki M., Yamashita T., Yano H., Tatsumi K., Aoki K. Differential scanning calorimetric studies on bovine serum albumin. IV. Effect of anionic surfactants with various lengths of hydrocarbon chain. Int. J. Biol. Macromol. 19:1996;241-246.
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 241-246
    • Yamasaki, M.1    Yamashita, T.2    Yano, H.3    Tatsumi, K.4    Aoki, K.5
  • 30
    • 0035255916 scopus 로고    scopus 로고
    • Morphology, drug distribution, and in vitro release profiles of biodegradable polymeric microspheres containing protein fabricated by double-emulsion solvent extraction/evaporation method
    • Yang Y.Y., Chung T.S., Ng N.P. Morphology, drug distribution, and in vitro release profiles of biodegradable polymeric microspheres containing protein fabricated by double-emulsion solvent extraction/evaporation method. Biomaterials. 22:2001;231-241.
    • (2001) Biomaterials , vol.22 , pp. 231-241
    • Yang, Y.Y.1    Chung, T.S.2    Ng, N.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.