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Volumn 98, Issue , 2012, Pages 80-84

Characterization and side effect analysis of a newly designed nanoemulsion targeting human serum albumin for drug delivery

Author keywords

Drug carrier; HSA; Intrinsic fluorescence; Nanoemulsion; Side effect

Indexed keywords

DRUG CARRIER; HSA; INTRINSIC FLUORESCENCE; NANOEMULSION; SIDE EFFECT;

EID: 84861558520     PISSN: 09277765     EISSN: 18734367     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2012.04.036     Document Type: Article
Times cited : (36)

References (24)
  • 1
    • 0028227096 scopus 로고
    • Structure and ligand binding properties of human serum albumin
    • Caterand D.C., Ho J.X. Structure and ligand binding properties of human serum albumin. Adv. Protein Chem. 1994, 45:153-203.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Caterand, D.C.1    Ho, J.X.2
  • 2
    • 0032560039 scopus 로고    scopus 로고
    • Interaction of cisplatin with human serum albumin. Drug binding mode and protein secondary structure
    • Neault J.F., Tajmir-Riahi H.A. Interaction of cisplatin with human serum albumin. Drug binding mode and protein secondary structure. Biochim. Biophys. Acta 1998, 1384:153-159.
    • (1998) Biochim. Biophys. Acta , vol.1384 , pp. 153-159
    • Neault, J.F.1    Tajmir-Riahi, H.A.2
  • 3
    • 33846240498 scopus 로고    scopus 로고
    • Effect of human serum albumin on drug metabolism: structural evidence of esterase activity of human serum albumin
    • Yang F., Bian C., Zhu L., Zhao G., Huang Z., Huang M. Effect of human serum albumin on drug metabolism: structural evidence of esterase activity of human serum albumin. J. Struct. Biol. 2007, 157:348-355.
    • (2007) J. Struct. Biol. , vol.157 , pp. 348-355
    • Yang, F.1    Bian, C.2    Zhu, L.3    Zhao, G.4    Huang, Z.5    Huang, M.6
  • 4
    • 56949084877 scopus 로고    scopus 로고
    • Albumin as a drug carrier: design of prodrugs, drug conjugates and nanoparticles
    • Kratz F. Albumin as a drug carrier: design of prodrugs, drug conjugates and nanoparticles. J. Control. Release 2008, 132:171-183.
    • (2008) J. Control. Release , vol.132 , pp. 171-183
    • Kratz, F.1
  • 5
    • 77954756913 scopus 로고    scopus 로고
    • Interaction between a potent corticosteroid drug - dexamethasone with bovine serum albumin and human serum albumin: a fluorescence quenching and Fourier transformation infrared spectroscopy study
    • Naik N.S., Chimatadar A., Nandibewoor S.T. Interaction between a potent corticosteroid drug - dexamethasone with bovine serum albumin and human serum albumin: a fluorescence quenching and Fourier transformation infrared spectroscopy study. J. Photochem. Photobiol. B: Biol. 2010, 100:147-159.
    • (2010) J. Photochem. Photobiol. B: Biol. , vol.100 , pp. 147-159
    • Naik, N.S.1    Chimatadar, A.2    Nandibewoor, S.T.3
  • 6
    • 36549054137 scopus 로고    scopus 로고
    • Human serum albumin (HSA) nanoparticles: reproducibility of preparation process and kinetics of enzymatic degradation
    • Langer K., Anhorn M.G., Steinhauser L., Dreis S., Celebi D., Schrickel N., Faust S., Vogel V. Human serum albumin (HSA) nanoparticles: reproducibility of preparation process and kinetics of enzymatic degradation. Int. J. Pharm. 2008, 347:109-117.
    • (2008) Int. J. Pharm. , vol.347 , pp. 109-117
    • Langer, K.1    Anhorn, M.G.2    Steinhauser, L.3    Dreis, S.4    Celebi, D.5    Schrickel, N.6    Faust, S.7    Vogel, V.8
  • 7
    • 0019538149 scopus 로고
    • Molecular aspects of ligand binding to serum albumin
    • Kragh-Hansen U. Molecular aspects of ligand binding to serum albumin. Pharmacol. Rev. 1981, 33:17-53.
    • (1981) Pharmacol. Rev. , vol.33 , pp. 17-53
    • Kragh-Hansen, U.1
  • 8
    • 38849111818 scopus 로고    scopus 로고
    • Cytotoxicity of nanoparticles
    • Lewinski N., Colvin V., Drezek R. Cytotoxicity of nanoparticles. Small 2008, 4:26-49.
    • (2008) Small , vol.4 , pp. 26-49
    • Lewinski, N.1    Colvin, V.2    Drezek, R.3
  • 13
    • 0000814919 scopus 로고
    • Direct determination of absolute circular dichroism data and calibration of commercial instrument
    • Yang J.T., Wu C.S.C., Martinez H.M. Direct determination of absolute circular dichroism data and calibration of commercial instrument. Anal. Chem. 1981, 53:778.
    • (1981) Anal. Chem. , vol.53 , pp. 778
    • Yang, J.T.1    Wu, C.S.C.2    Martinez, H.M.3
  • 14
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra
    • Manavalan P., Johnson C.J.R. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 1987, 167:76-85.
    • (1987) Anal. Biochem. , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson, C.J.R.2
  • 15
    • 79953653213 scopus 로고    scopus 로고
    • Mannosylated chitosan-zinc sulphide nanocrystals as fluorescent bioprobes for targeted cancer imaging
    • Jayasree A., Sasidharan S., Koyakutty M., Nair S., Menon M. Mannosylated chitosan-zinc sulphide nanocrystals as fluorescent bioprobes for targeted cancer imaging. Carbohydr. Polym. 2011, 85:37-43.
    • (2011) Carbohydr. Polym. , vol.85 , pp. 37-43
    • Jayasree, A.1    Sasidharan, S.2    Koyakutty, M.3    Nair, S.4    Menon, M.5
  • 16
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • Vivian J.T., Callis P.R. Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J. 2001, 80:2093-2109.
    • (2001) Biophys. J. , vol.80 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 17
    • 77957750387 scopus 로고    scopus 로고
    • Spectroscopic and nano-molecular modeling investigation on the binary and ternary bindings of colchicine and lomefloxacin to human serum albumin with the viewpoint of multi-drug therapy
    • Chamani J., Asoodeh A., Homayoni-Tabrizi M., AmiriTehranizadeh Z., Baratian A., Saberi M.R., Gharanfoli M. Spectroscopic and nano-molecular modeling investigation on the binary and ternary bindings of colchicine and lomefloxacin to human serum albumin with the viewpoint of multi-drug therapy. J. Lumin. 2010, 130:2476-2486.
    • (2010) J. Lumin. , vol.130 , pp. 2476-2486
    • Chamani, J.1    Asoodeh, A.2    Homayoni-Tabrizi, M.3    AmiriTehranizadeh, Z.4    Baratian, A.5    Saberi, M.R.6    Gharanfoli, M.7
  • 18
    • 0033135193 scopus 로고    scopus 로고
    • 1-Anilino-8-naphthalene sulfonate as a protein conformational tightening agent
    • Matulis D., Baumann C.G., Bloomfield V.A., Lovrien R.E. 1-Anilino-8-naphthalene sulfonate as a protein conformational tightening agent. Biopolymers 1999, 49:451-458.
    • (1999) Biopolymers , vol.49 , pp. 451-458
    • Matulis, D.1    Baumann, C.G.2    Bloomfield, V.A.3    Lovrien, R.E.4
  • 19
    • 33646159747 scopus 로고    scopus 로고
    • ANS fluorescence detects widespread perturbations of protein tertiary structure in ice
    • Gabellieri E., Strambini G.B. ANS fluorescence detects widespread perturbations of protein tertiary structure in ice. Biophys. J. 2006, 90:3239-3245.
    • (2006) Biophys. J. , vol.90 , pp. 3239-3245
    • Gabellieri, E.1    Strambini, G.B.2
  • 20
    • 0033135193 scopus 로고    scopus 로고
    • 1-Anilino-8-naphthalene sulfonate as a protein conformational tightening agent
    • Matulis D., Baumann C.G., Bloomfield V.A., Lovrien R.E. 1-Anilino-8-naphthalene sulfonate as a protein conformational tightening agent. Biopolymers 1999, 49:451-458.
    • (1999) Biopolymers , vol.49 , pp. 451-458
    • Matulis, D.1    Baumann, C.G.2    Bloomfield, V.A.3    Lovrien, R.E.4
  • 21
    • 76249105826 scopus 로고    scopus 로고
    • Complexes of dendrimers with bovine serum albumin
    • Mandeville J.S., Tajmir-Riahi H.A. Complexes of dendrimers with bovine serum albumin. Biomacromolecules 2010, 11:465-472.
    • (2010) Biomacromolecules , vol.11 , pp. 465-472
    • Mandeville, J.S.1    Tajmir-Riahi, H.A.2
  • 23
    • 59049106309 scopus 로고    scopus 로고
    • Study of curcumin and genistein interactions with human serum albumin
    • Mandeville J.S., Tajmir-Riahi H.A. Study of curcumin and genistein interactions with human serum albumin. J. Pharm. Biomed. Anal. 2009, 49:468-474.
    • (2009) J. Pharm. Biomed. Anal. , vol.49 , pp. 468-474
    • Mandeville, J.S.1    Tajmir-Riahi, H.A.2
  • 24
    • 61949432567 scopus 로고    scopus 로고
    • Structural analysis of human serum albumin complexes with cationic lipids
    • Charbonneau D., Beauregard M., Tajmir-Riahi H.A. Structural analysis of human serum albumin complexes with cationic lipids. J. Phys. Chem. B 2009, 113:1777-1784.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 1777-1784
    • Charbonneau, D.1    Beauregard, M.2    Tajmir-Riahi, H.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.