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Volumn 429, Issue , 2012, Pages 156-160

Interaction and nanotoxic effect of TiO 2 nanoparticle on fibrinogen by multi-spectroscopic method

Author keywords

Binding constant; Nanotoxicology; Protein nanoparticle interaction; TiO 2 nanoparticles

Indexed keywords

BINDING CONSTANT; CONFORMATIONAL CHANGE; COOPERATIVITY; DAILY LIVES; ENVIRONMENTAL EXPOSURE; FLUORESCENCE QUENCHING; FUNCTIONAL PROTEINS; HUMAN HEALTH; NANOTOXICOLOGY; PHOTOPHYSICAL MEASUREMENTS; PHYSICOCHEMICAL CHARACTERISTICS; PROTEIN-NANOPARTICLE INTERACTION; TIO; TOXICOLOGICAL EFFECTS;

EID: 84862263586     PISSN: 00489697     EISSN: 18791026     Source Type: Journal    
DOI: 10.1016/j.scitotenv.2012.03.048     Document Type: Article
Times cited : (26)

References (34)
  • 2
    • 20644449754 scopus 로고    scopus 로고
    • Nanotoxicology: an emerging discipline evolving from studies of ultrafine particles
    • Oberdörster G., Oberdörster E., Oberdörster J. Nanotoxicology: an emerging discipline evolving from studies of ultrafine particles. Environ Health Perspect 2005, 113:823-839.
    • (2005) Environ Health Perspect , vol.113 , pp. 823-839
    • Oberdörster, G.1    Oberdörster, E.2    Oberdörster, J.3
  • 4
    • 77949291428 scopus 로고    scopus 로고
    • 2 with lysozyme: insights into the enzyme toxicity of nanosized particles
    • 2 with lysozyme: insights into the enzyme toxicity of nanosized particles. Environ Sci Pollut Res 2011, 17:798-806.
    • (2011) Environ Sci Pollut Res , vol.17 , pp. 798-806
    • Xu, Z.1    Liu, X.W.2    Ma, Y.S.3    Gao, H.W.4
  • 6
    • 71949117632 scopus 로고    scopus 로고
    • Safety assessment for nanotechnology and nanomedicine: concepts of nanotoxicology
    • Oberdörster G. Safety assessment for nanotechnology and nanomedicine: concepts of nanotoxicology. J Intern Med 2010, 267:89-105.
    • (2010) J Intern Med , vol.267 , pp. 89-105
    • Oberdörster, G.1
  • 7
    • 33845218637 scopus 로고    scopus 로고
    • In vitro toxicity of silica nanoparticles in human lung cancer cells
    • Lin W.S., Huang Y.W., Zhou X.D., Ma Y.F. In vitro toxicity of silica nanoparticles in human lung cancer cells. Toxicol Appl Pharmacol 2006, 217:252-259.
    • (2006) Toxicol Appl Pharmacol , vol.217 , pp. 252-259
    • Lin, W.S.1    Huang, Y.W.2    Zhou, X.D.3    Ma, Y.F.4
  • 8
    • 77957935560 scopus 로고    scopus 로고
    • Physico-chemical features of engineered nanoparticles relevant to their toxicity
    • Fubini B., Ghiazza M., Fenoglio I. Physico-chemical features of engineered nanoparticles relevant to their toxicity. Nanotoxicology 2010, 4:347-363.
    • (2010) Nanotoxicology , vol.4 , pp. 347-363
    • Fubini, B.1    Ghiazza, M.2    Fenoglio, I.3
  • 9
    • 80051483471 scopus 로고    scopus 로고
    • The effects of serum on the toxicity of manufactured nanoparticles
    • Clift M.J.D., Bhattacharjee S., Brown D.M., Vicki S. The effects of serum on the toxicity of manufactured nanoparticles. Toxicol Lett 2010, 198:358-365.
    • (2010) Toxicol Lett , vol.198 , pp. 358-365
    • Clift, M.J.D.1    Bhattacharjee, S.2    Brown, D.M.3    Vicki, S.4
  • 10
  • 11
    • 77957875614 scopus 로고    scopus 로고
    • Mechanisms and measurements of nanomaterial -induced oxidative damage to DNA
    • Petersen E.J., Nelson B.C. Mechanisms and measurements of nanomaterial -induced oxidative damage to DNA. Anal Bioanal Chem 2010, 398:613-650.
    • (2010) Anal Bioanal Chem , vol.398 , pp. 613-650
    • Petersen, E.J.1    Nelson, B.C.2
  • 13
    • 79960955443 scopus 로고    scopus 로고
    • DNA exposure to Buckminsterfullerene (C60): toward DNA stability, reactivity, and replication
    • Jie H., Jin B. DNA exposure to Buckminsterfullerene (C60): toward DNA stability, reactivity, and replication. Environ Sci Technol 2011, 45:6608-6616.
    • (2011) Environ Sci Technol , vol.45 , pp. 6608-6616
    • Jie, H.1    Jin, B.2
  • 14
  • 15
    • 77956224283 scopus 로고    scopus 로고
    • Effects of nano-sized silicon dioxide on the structures and activities of three functional proteins
    • Xu Z., Wang S.L., Gao H.W. Effects of nano-sized silicon dioxide on the structures and activities of three functional proteins. J Hazard Mater 2010, 180:375-383.
    • (2010) J Hazard Mater , vol.180 , pp. 375-383
    • Xu, Z.1    Wang, S.L.2    Gao, H.W.3
  • 16
    • 33847789142 scopus 로고    scopus 로고
    • Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles
    • Cedervall T., Lynch I., Lindman S., Berggård T., Thulin E., Nilsson H., Dawson K.A., Linse S. Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci USA 2007, 104:2050-2055.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2050-2055
    • Cedervall, T.1    Lynch, I.2    Lindman, S.3    Berggård, T.4    Thulin, E.5    Nilsson, H.6    Dawson, K.A.7    Linse, S.8
  • 17
    • 34248342939 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction between human hemoglobin and Cd quantum dots
    • Shen X.C., Liou X.Y., Ye L.P., Liang H., Wang Z.Y. Spectroscopic studies on the interaction between human hemoglobin and Cd quantum dots. J Colloid Interface Sci 2007, 311:400-406.
    • (2007) J Colloid Interface Sci , vol.311 , pp. 400-406
    • Shen, X.C.1    Liou, X.Y.2    Ye, L.P.3    Liang, H.4    Wang, Z.Y.5
  • 19
    • 78649447265 scopus 로고    scopus 로고
    • Mechanisms of fibrinogen-acebutolol interactions: insights from DSC, CD and LS
    • Hassana N., Rusoa J.M., Somasundaran P. Mechanisms of fibrinogen-acebutolol interactions: insights from DSC, CD and LS. Colloids Surf B 2011, 82:581-587.
    • (2011) Colloids Surf B , vol.82 , pp. 581-587
    • Hassana, N.1    Rusoa, J.M.2    Somasundaran, P.3
  • 21
    • 67049158447 scopus 로고    scopus 로고
    • Interaction of fibrin(ogen) with the endothelial cell receptor VE-cadherin: localization of the fibrin-binding site within the third extracellular VE-Cadherin domain
    • Yakovlev S., Medved L. Interaction of fibrin(ogen) with the endothelial cell receptor VE-cadherin: localization of the fibrin-binding site within the third extracellular VE-Cadherin domain. Biochemistry 2009, 48:5171-5179.
    • (2009) Biochemistry , vol.48 , pp. 5171-5179
    • Yakovlev, S.1    Medved, L.2
  • 23
    • 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 P.N., Chimatadar S.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 2010, 100:147-159.
    • (2010) J Photochem Photobiol B , vol.100 , pp. 147-159
    • Naik, P.N.1    Chimatadar, S.A.2    Nandibewoor, S.T.3
  • 24
    • 65049085725 scopus 로고    scopus 로고
    • Study of protein-gold nanoparticle conjugates by fluorescence and surface-enhanced Raman scattering
    • Iosin M., Toderas F., Baldeck P.L., Astilean S. Study of protein-gold nanoparticle conjugates by fluorescence and surface-enhanced Raman scattering. J Mol Struct 2009, 924-926:196-200.
    • (2009) J Mol Struct , pp. 196-200
    • Iosin, M.1    Toderas, F.2    Baldeck, P.L.3    Astilean, S.4
  • 25
    • 78649631100 scopus 로고    scopus 로고
    • Study of interaction of butyl p-hydroxybenzoate with human serum albumin by molecular modeling and multi-spectroscopic method
    • Wang Q., Zhang Y.H., Sun H.J., Chen H.L., Chen X.G. Study of interaction of butyl p-hydroxybenzoate with human serum albumin by molecular modeling and multi-spectroscopic method. J Lumin 2011, 131:206-211.
    • (2011) J Lumin , vol.131 , pp. 206-211
    • Wang, Q.1    Zhang, Y.H.2    Sun, H.J.3    Chen, H.L.4    Chen, X.G.5
  • 26
    • 0032478116 scopus 로고    scopus 로고
    • Tryptophan fluorescence quenching by methionine and selenomethionine residues of calmodulin: orientation of peptide and protein binding
    • Yuan T., Weljie A.M., Vogel H.J. Tryptophan fluorescence quenching by methionine and selenomethionine residues of calmodulin: orientation of peptide and protein binding. Biochemistry 1998, 37:3187-3195.
    • (1998) Biochemistry , vol.37 , pp. 3187-3195
    • Yuan, T.1    Weljie, A.M.2    Vogel, H.J.3
  • 27
    • 84969001783 scopus 로고
    • The attractions of protein for small molecules and ions
    • Scatchard G. The attractions of protein for small molecules and ions. Ann NY Acad Sci 1949, 51:660-673.
    • (1949) Ann NY Acad Sci , vol.51 , pp. 660-673
    • Scatchard, G.1
  • 29
    • 0034737805 scopus 로고    scopus 로고
    • Studies on the interactions between human serum albumin and transindazolium (bisindazole) tetrachlororuthenate(III)
    • Trynda-Lemiesz L., Karaczyn A., Keppler B.K., Koztowski H. Studies on the interactions between human serum albumin and transindazolium (bisindazole) tetrachlororuthenate(III). J Inorg Biochem 2000, 78:341-346.
    • (2000) J Inorg Biochem , vol.78 , pp. 341-346
    • Trynda-Lemiesz, L.1    Karaczyn, A.2    Keppler, B.K.3    Koztowski, H.4
  • 31
    • 33750176864 scopus 로고    scopus 로고
    • Comparison of the characterization on binding of alpinetin and cardamonin to lysozyme by spectroscopic methods
    • He W.Y., Li Y., Tang J.H., Luan F., Jin J., Hu Z.D. Comparison of the characterization on binding of alpinetin and cardamonin to lysozyme by spectroscopic methods. Int J Biol Macromol 2007, 39:165-173.
    • (2007) Int J Biol Macromol , vol.39 , pp. 165-173
    • He, W.Y.1    Li, Y.2    Tang, J.H.3    Luan, F.4    Jin, J.5    Hu, Z.D.6
  • 32
    • 33645133250 scopus 로고    scopus 로고
    • Research strategies for safety evaluation of nanomaterials. Part VI. Characterization of nanoscale particles for toxicological evaluation
    • Powers K.W., Brown S.C., Krishna V.B., Wasdo S.C., Moudgil B.M., Roberts S.M. Research strategies for safety evaluation of nanomaterials. Part VI. Characterization of nanoscale particles for toxicological evaluation. Toxicol Sci 2006, 90:296-303.
    • (2006) Toxicol Sci , vol.90 , pp. 296-303
    • Powers, K.W.1    Brown, S.C.2    Krishna, V.B.3    Wasdo, S.C.4    Moudgil, B.M.5    Roberts, S.M.6
  • 33
    • 67349191427 scopus 로고    scopus 로고
    • Interaction of colloidal gold nanoparticles with human blood: effects on particle size and analysis of plasma protein binding profiles
    • Clogston J.D., Ayub N., Aggarwal P., Neun B.W., Hall J.B., McNeil S.E. Interaction of colloidal gold nanoparticles with human blood: effects on particle size and analysis of plasma protein binding profiles. Nanomed Nanotechnol Biol Med 2009, 5:106-117.
    • (2009) Nanomed Nanotechnol Biol Med , vol.5 , pp. 106-117
    • Clogston, J.D.1    Ayub, N.2    Aggarwal, P.3    Neun, B.W.4    Hall, J.B.5    McNeil, S.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.