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Volumn 95, Issue 12, 2006, Pages 2722-2729

Effects of cyclodextrins on chemically and thermally induced unfolding and aggregation of lysozyme and basic fibroblast growth factor

Author keywords

Aggregation; Basic fibroblast growth factor; Cyclodextrins; Lysozyme; Unfolding

Indexed keywords

BASIC FIBROBLAST GROWTH FACTOR; BETA CYCLODEXTRIN; BETA CYCLODEXTRIN SULFOBUTYL ETHER; CYCLODEXTRIN DERIVATIVE; DIMETHYL BETA CYCLODEXTRIN; LYSOZYME; MALTOSE; PHOSPHATE BUFFERED SALINE; UNCLASSIFIED DRUG;

EID: 33846185130     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.20715     Document Type: Article
Times cited : (51)

References (23)
  • 1
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W. 2005. Protein aggregation and its inhibition in biopharmaceutics. Int J Pharm 289:1-30.
    • (2005) Int J Pharm , vol.289 , pp. 1-30
    • Wang, W.1
  • 2
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: News insight into protein folding, misfolding diseases and biological evolutaion
    • Stefani M, Dobson CM. 2003. Protein aggregation and aggregate toxicity: News insight into protein folding, misfolding diseases and biological evolutaion. J Mol Med 81:689-699.
    • (2003) J Mol Med , vol.81 , pp. 689-699
    • Stefani, M.1    Dobson, C.M.2
  • 3
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization-induced and temperature-induced protein aggregation
    • Dong AC, Prestrelski SJ, Allison SD, Carpenter JF. 1995. Infrared spectroscopic studies of lyophilization-induced and temperature-induced protein aggregation. J Pharm Sci 84:415-424.
    • (1995) J Pharm Sci , vol.84 , pp. 415-424
    • Dong, A.C.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 4
  • 5
    • 0346331895 scopus 로고    scopus 로고
    • Stressed-out B cells? Plasma-cell differentiation and the unfolded protein response
    • Gass JN, Gunn KE, Sriburiand R, Brewer JW. 2004. Stressed-out B cells? Plasma-cell differentiation and the unfolded protein response. Trends Immunol 25:17-24.
    • (2004) Trends Immunol , vol.25 , pp. 17-24
    • Gass, J.N.1    Gunn, K.E.2    Sriburiand, R.3    Brewer, J.W.4
  • 6
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: A formulation challenge
    • Frokjaer S, Otzen DE. 2005. Protein drug stability: A formulation challenge. Nat Rev Drug Discov 4:298-306.
    • (2005) Nat Rev Drug Discov , vol.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 7
    • 1442359491 scopus 로고    scopus 로고
    • Structural background of cyclodextrin-protein interactions
    • Aachmann FL, Otzen DE, Larsen KL, Wimmer R. 2003. Structural background of cyclodextrin-protein interactions. Protein Eng 16:905-912.
    • (2003) Protein Eng , vol.16 , pp. 905-912
    • Aachmann, F.L.1    Otzen, D.E.2    Larsen, K.L.3    Wimmer, R.4
  • 9
    • 0001357555 scopus 로고
    • Biopharmaceutical evaluation of maltosyl-β-cyclodextrin as a parenteral drug carrier
    • Yamamoto M, Aritomi H, Irie T, Hirayama F, Uekama K. 1991. Biopharmaceutical evaluation of maltosyl-β-cyclodextrin as a parenteral drug carrier. STP Pharma Sci 1:397-402.
    • (1991) STP Pharma Sci , vol.1 , pp. 397-402
    • Yamamoto, M.1    Aritomi, H.2    Irie, T.3    Hirayama, F.4    Uekama, K.5
  • 11
    • 0028215217 scopus 로고
    • Chromatographic methods for quantitation of native, denatured and aggregated bFGF in solution formulations
    • Sluzky V, Shahrokh Z, Stratton PA, Eberlein GA, Wang J. 1994. Chromatographic methods for quantitation of native, denatured and aggregated bFGF in solution formulations. Pharm Res 11:485-490.
    • (1994) Pharm Res , vol.11 , pp. 485-490
    • Sluzky, V.1    Shahrokh, Z.2    Stratton, P.A.3    Eberlein, G.A.4    Wang, J.5
  • 12
    • 0035988096 scopus 로고    scopus 로고
    • Cooperative effects of artificial chaperones and guanidium chloride on lysozyme renaturation at high concentrations
    • Dong X, Shi J, Sun Y. 2002. Cooperative effects of artificial chaperones and guanidium chloride on lysozyme renaturation at high concentrations. Biotechnol Prog 18:663-665.
    • (2002) Biotechnol Prog , vol.18 , pp. 663-665
    • Dong, X.1    Shi, J.2    Sun, Y.3
  • 13
    • 17644384876 scopus 로고    scopus 로고
    • Effects of hydrophilic cyclodextrins on aggregation of recombinant human growth hormone
    • Tavornvipas S, Tajiri S, Hirayama F, Arima H, Uekama K. 2004. Effects of hydrophilic cyclodextrins on aggregation of recombinant human growth hormone. Pharm Res 21:2369-2376.
    • (2004) Pharm Res , vol.21 , pp. 2369-2376
    • Tavornvipas, S.1    Tajiri, S.2    Hirayama, F.3    Arima, H.4    Uekama, K.5
  • 14
    • 0032901515 scopus 로고    scopus 로고
    • Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition
    • Jelesarov I, Bosshard HR. 1999. Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J Mol Recognit 12:3-18.
    • (1999) J Mol Recognit , vol.12 , pp. 3-18
    • Jelesarov, I.1    Bosshard, H.R.2
  • 15
    • 0026459045 scopus 로고
    • Effect of cyclodextrins on the thermal stability of globular proteins
    • Cooper A. 1992. Effect of cyclodextrins on the thermal stability of globular proteins. J Am Chem Soc 114:9208-9209.
    • (1992) J Am Chem Soc , vol.114 , pp. 9208-9209
    • Cooper, A.1
  • 16
    • 0020477017 scopus 로고
    • Stabilization of protein structure by Sugars
    • Arakawa T, Timasheff SN. 1992. Stabilization of protein structure by Sugars. Biochemistry 21:6536-6544.
    • (1992) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 17
    • 0037466513 scopus 로고    scopus 로고
    • The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation
    • Arakawa T, Tsumoto K. 2003. The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation. Biochem Biophys Res Comm 304:148-152.
    • (2003) Biochem Biophys Res Comm , vol.304 , pp. 148-152
    • Arakawa, T.1    Tsumoto, K.2
  • 18
    • 0026716134 scopus 로고
    • Stabilization of basic fibroblast growth factor with dextran sulfate
    • Kajio T, Kawahara K, Kato K. 1992. Stabilization of basic fibroblast growth factor with dextran sulfate. FEBS Lett 306:243-246.
    • (1992) FEBS Lett , vol.306 , pp. 243-246
    • Kajio, T.1    Kawahara, K.2    Kato, K.3
  • 19
    • 0028325205 scopus 로고
    • Aluminium β-cyclodextrin sulphate as a stabilizer and sustained-release carrier for basic fibroblast growth factor
    • Fukunaga K, Hijikata S, Ishimura K, Sonoda R, Irie T, Uekama K. 1994. Aluminium β-cyclodextrin sulphate as a stabilizer and sustained-release carrier for basic fibroblast growth factor. J Pharm Pharmacol 46:168-171.
    • (1994) J Pharm Pharmacol , vol.46 , pp. 168-171
    • Fukunaga, K.1    Hijikata, S.2    Ishimura, K.3    Sonoda, R.4    Irie, T.5    Uekama, K.6
  • 21
    • 0022477372 scopus 로고
    • Heparin protects basic and acidic FGF from inactivation
    • Gospodarowicz D, Cheng J. 1986. Heparin protects basic and acidic FGF from inactivation. J Cell Physiol 128:475-484.
    • (1986) J Cell Physiol , vol.128 , pp. 475-484
    • Gospodarowicz, D.1    Cheng, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.