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Volumn 373, Issue 1-2, 2009, Pages 107-115

Evaluation of pharmacological efficacy of 'insulin-surfoplex' encapsulated polymer vesicles

Author keywords

In vitro and in vivo evaluation; Insulin; Ion pair complex; Polymerosomes; Surfactant

Indexed keywords

DEOXYCHOLATE SODIUM; EPSILON CAPROLACTONE; MACROGOL 2000; NANOPARTICLE; POLYCAPROLACTONE; RECOMBINANT HUMAN INSULIN; RECOMBINANT HUMAN INSULIN EPSILON CAPROLACTONE MACROGOL 2000 CONJUGATE; SURFACTANT; UNCLASSIFIED DRUG;

EID: 67349152349     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2009.01.022     Document Type: Article
Times cited : (21)

References (22)
  • 1
    • 14844317382 scopus 로고    scopus 로고
    • Strategic approaches for overcoming peptide and protein instability within biodegradable nano- and microparticles
    • Bilati U., Allémann E., and Doelker E. Strategic approaches for overcoming peptide and protein instability within biodegradable nano- and microparticles. Eur. J. Pharm. Biopharm. 59 (2005) 375-388
    • (2005) Eur. J. Pharm. Biopharm. , vol.59 , pp. 375-388
    • Bilati, U.1    Allémann, E.2    Doelker, E.3
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0034255054 scopus 로고    scopus 로고
    • Hydrophobic ion pair formation between leuprolide and sodium oleate for sustained release from biodegradable polymeric microspheres
    • Choi S.H., and Park T.G. Hydrophobic ion pair formation between leuprolide and sodium oleate for sustained release from biodegradable polymeric microspheres. Int. J. Pharm. 203 (2000) 193-202
    • (2000) Int. J. Pharm. , vol.203 , pp. 193-202
    • Choi, S.H.1    Park, T.G.2
  • 4
    • 4544233671 scopus 로고    scopus 로고
    • Correlations induce association in polyelectrolyte solutions
    • da Silva M.B., Lucena L.S., and Barbosa M.C. Correlations induce association in polyelectrolyte solutions. Physica A 342 (2004) 54-61
    • (2004) Physica A , vol.342 , pp. 54-61
    • da Silva, M.B.1    Lucena, L.S.2    Barbosa, M.C.3
  • 5
    • 34047249414 scopus 로고    scopus 로고
    • Characterization of physiochemical and biological properties of an insulin/lauryl sulfate complex formed by hydrophobic ion pairing
    • Dai W.G., and Dong L.C. Characterization of physiochemical and biological properties of an insulin/lauryl sulfate complex formed by hydrophobic ion pairing. Int. J. Pharm. 336 (2007) 58-66
    • (2007) Int. J. Pharm. , vol.336 , pp. 58-66
    • Dai, W.G.1    Dong, L.C.2
  • 7
    • 0013889689 scopus 로고
    • Determination of free amino groups in proteins by trinitrobenzenesulfonic acid
    • Habeeb A.F.S.A. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Anal. Biochem. 14 (1966) 328-336
    • (1966) Anal. Biochem. , vol.14 , pp. 328-336
    • Habeeb, A.F.S.A.1
  • 8
    • 0001749410 scopus 로고    scopus 로고
    • Aggregation number for sodium deoxycholate from steady-state and time-resolved fluorescence
    • Jover A., Meijide F., Nunez E.R., Vazquez J., and Mosquera M. Aggregation number for sodium deoxycholate from steady-state and time-resolved fluorescence. Langmuir 13 (1997) 161-164
    • (1997) Langmuir , vol.13 , pp. 161-164
    • Jover, A.1    Meijide, F.2    Nunez, E.R.3    Vazquez, J.4    Mosquera, M.5
  • 9
    • 0014606996 scopus 로고
    • Diabetogenic action of streptozotocin: relationship of dose to metabolic response
    • Junod A., Lambert A.E., Stauffacher W., and Renold A.E. Diabetogenic action of streptozotocin: relationship of dose to metabolic response. J. Clin. Invest. 48 (1969) 2129-2139
    • (1969) J. Clin. Invest. , vol.48 , pp. 2129-2139
    • Junod, A.1    Lambert, A.E.2    Stauffacher, W.3    Renold, A.E.4
  • 10
    • 0031282463 scopus 로고    scopus 로고
    • Hydrophobic ion pairing as a method for enhancing structure and activity of lyophilized subtilisin bpn suspended in isooctane
    • Kendrick B.S., Meyer J.D., Matsuura J.E., Carpenter J.F., and Manning M.C. Hydrophobic ion pairing as a method for enhancing structure and activity of lyophilized subtilisin bpn suspended in isooctane. Arch. Biochem. Biophys. 347 (1997) 113-118
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 113-118
    • Kendrick, B.S.1    Meyer, J.D.2    Matsuura, J.E.3    Carpenter, J.F.4    Manning, M.C.5
  • 11
    • 0032526863 scopus 로고    scopus 로고
    • High-performance liquid chomatographic determination of insulin in rat and human plasma
    • Khaksa G., Nalini K., Bhat M., and Udupa N. High-performance liquid chomatographic determination of insulin in rat and human plasma. Anal. Biochem. 260 (1998) 92-95
    • (1998) Anal. Biochem. , vol.260 , pp. 92-95
    • Khaksa, G.1    Nalini, K.2    Bhat, M.3    Udupa, N.4
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of Bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0031915619 scopus 로고    scopus 로고
    • Hydrophobic ion pairing: altering the solubility properties of biomolecules
    • Meyer J.D., and Manning M.C. Hydrophobic ion pairing: altering the solubility properties of biomolecules. Pharm. Res. 15 (1998) 188-193
    • (1998) Pharm. Res. , vol.15 , pp. 188-193
    • Meyer, J.D.1    Manning, M.C.2
  • 14
    • 41249095351 scopus 로고    scopus 로고
    • Surfactant-induced amorphous aggregation of tobacco mosaic virus coat protein: a physical methods approach
    • Panyukov Y.V., Nemykh M.A., Dobrov E.N., and Drachev V.A. Surfactant-induced amorphous aggregation of tobacco mosaic virus coat protein: a physical methods approach. Macromol. Biosci. 8 (2008) 199-209
    • (2008) Macromol. Biosci. , vol.8 , pp. 199-209
    • Panyukov, Y.V.1    Nemykh, M.A.2    Dobrov, E.N.3    Drachev, V.A.4
  • 15
    • 0027607911 scopus 로고
    • Enhanced solubility of proteins and peptides in nonpolar solvents through hydrophobic ion pairing
    • Powers M.E., Matsuura J., Brassell J., Manning M.C., and Shefter E. Enhanced solubility of proteins and peptides in nonpolar solvents through hydrophobic ion pairing. Biopolymers 33 (1993) 927-932
    • (1993) Biopolymers , vol.33 , pp. 927-932
    • Powers, M.E.1    Matsuura, J.2    Brassell, J.3    Manning, M.C.4    Shefter, E.5
  • 17
    • 0023658288 scopus 로고
    • Chromatography of complex protein mixtures
    • Regnier F.E. Chromatography of complex protein mixtures. J. Chromatogr. 418 (1987) 115-143
    • (1987) J. Chromatogr. , vol.418 , pp. 115-143
    • Regnier, F.E.1
  • 18
    • 4644246567 scopus 로고    scopus 로고
    • Noninvasive methods to determine the critical micelle concentration of some bile acid salts
    • Reis S., Moutinho C.G., Matos C., de Castro B., Gameiro P., and Lima J.L.F.C. Noninvasive methods to determine the critical micelle concentration of some bile acid salts. Anal. Biochem. 334 (2004) 117-126
    • (2004) Anal. Biochem. , vol.334 , pp. 117-126
    • Reis, S.1    Moutinho, C.G.2    Matos, C.3    de Castro, B.4    Gameiro, P.5    Lima, J.L.F.C.6
  • 20
    • 0033635054 scopus 로고    scopus 로고
    • Protein instability in poly(lactic-co-glycolic acid) microparticles
    • van de Weert M., Hennink W.E., and Jiskoot W. Protein instability in poly(lactic-co-glycolic acid) microparticles. Pharm. Res. 17 (2000) 1159-1167
    • (2000) Pharm. Res. , vol.17 , pp. 1159-1167
    • van de Weert, M.1    Hennink, W.E.2    Jiskoot, W.3
  • 21
    • 34548288653 scopus 로고    scopus 로고
    • Native PAGE eliminates the problem of PEG-SDS interaction in SDS-PAGE and provides an alternative to HPLC in characterization of protein PEGylation
    • Zheng C.Y., Ma G., and Su Z. Native PAGE eliminates the problem of PEG-SDS interaction in SDS-PAGE and provides an alternative to HPLC in characterization of protein PEGylation. Electrophoresis 28 (2007) 2801-2807
    • (2007) Electrophoresis , vol.28 , pp. 2801-2807
    • Zheng, C.Y.1    Ma, G.2    Su, Z.3
  • 22
    • 0038384496 scopus 로고    scopus 로고
    • Biodegradable poly(ε-caprolactone)-poly(ethylene glycol) block copolymers: characterization and their use as drug carriers for a controlled delivery system
    • Zhou S., Deng X., and Yang H. Biodegradable poly(ε-caprolactone)-poly(ethylene glycol) block copolymers: characterization and their use as drug carriers for a controlled delivery system. Biomaterials 24 (2003) 3563-3570
    • (2003) Biomaterials , vol.24 , pp. 3563-3570
    • Zhou, S.1    Deng, X.2    Yang, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.