메뉴 건너뛰기




Volumn 8, Issue 1, 2012, Pages 119-129

Cross-linked antioxidant nanozymes for improved delivery to CNS

Author keywords

Brain delivery; Cross linking; Nanozymes; Polyion complexes

Indexed keywords

ANTIOXIDANT ENZYME; BRAIN DELIVERY; BRAIN TISSUE; CARBODIIMIDE HYDROCHLORIDES; CENTRAL NERVOUS SYSTEMS; CHARGE RATIO; COVALENT CROSSLINKING; CU/ZN-SOD; ELECTROSTATIC COUPLING; GEL ELECTROPHORESIS; GLUTARALDEHYDES; IN-VIVO; L-LYSINE; NANOZYMES; NEUROLOGICAL DISEASE; PHYSICO-CHEMICAL CHARACTERIZATION; POLYCATIONS; POLYION COMPLEX; REACTION CONDITIONS; SODIUM SALT; SUPER OXIDE DISMUTASE; WESTERN BLOTTING;

EID: 84855309939     PISSN: 15499634     EISSN: 15499642     Source Type: Journal    
DOI: 10.1016/j.nano.2011.05.010     Document Type: Article
Times cited : (71)

References (44)
  • 1
    • 29744450671 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor is neuroprotective against human immunodeficiency virus-1 envelope proteins
    • Bachis A., Mocchetti I. Brain-derived neurotrophic factor is neuroprotective against human immunodeficiency virus-1 envelope proteins. Ann N Y Acad Sci 2005, 1053:247-257.
    • (2005) Ann N Y Acad Sci , vol.1053 , pp. 247-257
    • Bachis, A.1    Mocchetti, I.2
  • 2
    • 0037225431 scopus 로고    scopus 로고
    • Neuroprotective effects of IGF-I against TNFalpha-induced neuronal damage in HIV-associated dementia
    • Ying Wang J., Peruzzi F., Lassak A., Del Valle L., Radhakrishnan S., Rappaport J., et al. Neuroprotective effects of IGF-I against TNFalpha-induced neuronal damage in HIV-associated dementia. Virology 2003, 305:66-76.
    • (2003) Virology , vol.305 , pp. 66-76
    • Ying Wang, J.1    Peruzzi, F.2    Lassak, A.3    Del Valle, L.4    Radhakrishnan, S.5    Rappaport, J.6
  • 3
    • 0036800457 scopus 로고    scopus 로고
    • HIV-1-associated dementia: a metabolic encephalopathy perpetrated by virus-infected and immune-competent mononuclear phagocytes
    • Anderson E., Zink W., Xiong H., Gendelman H.E. HIV-1-associated dementia: a metabolic encephalopathy perpetrated by virus-infected and immune-competent mononuclear phagocytes. J Acquir Immune Defic Syndr 2002, 31(Suppl 2):S43-S54.
    • (2002) J Acquir Immune Defic Syndr , vol.31 , Issue.SUPPL. 2
    • Anderson, E.1    Zink, W.2    Xiong, H.3    Gendelman, H.E.4
  • 4
    • 84855329640 scopus 로고    scopus 로고
    • Role of developmental inflammation and blood-brain barrier dysfunction in neurodevelopmental and neurodegenerative diseases
    • Stolp H., Dziegielewska K. Role of developmental inflammation and blood-brain barrier dysfunction in neurodevelopmental and neurodegenerative diseases. Neuropathol Appl Neurobiol 2008.
    • (2008) Neuropathol Appl Neurobiol
    • Stolp, H.1    Dziegielewska, K.2
  • 5
    • 0032875858 scopus 로고    scopus 로고
    • A women's health issue: Alzheimer's disease and strategies for maintaining cognitive health
    • Brinton R.D. A women's health issue: Alzheimer's disease and strategies for maintaining cognitive health. Int J Fertil Womens Med 1999, 44:174-185.
    • (1999) Int J Fertil Womens Med , vol.44 , pp. 174-185
    • Brinton, R.D.1
  • 6
    • 0035576894 scopus 로고    scopus 로고
    • Neuroprotective peptide drug delivery and development: potential new therapeutics
    • Gozes I. Neuroprotective peptide drug delivery and development: potential new therapeutics. Trends Neurosci 2001, 24:700-705.
    • (2001) Trends Neurosci , vol.24 , pp. 700-705
    • Gozes, I.1
  • 7
    • 0031965788 scopus 로고    scopus 로고
    • Outwitting the blood-brain barrier for therapeutic purposes: osmotic opening and other means
    • [discussion 99-100]
    • Kroll R.A., Neuwelt E.A. Outwitting the blood-brain barrier for therapeutic purposes: osmotic opening and other means. Neurosurgery 1998, 42:1083-1099. [discussion 99-100].
    • (1998) Neurosurgery , vol.42 , pp. 1083-1099
    • Kroll, R.A.1    Neuwelt, E.A.2
  • 8
    • 0025718569 scopus 로고
    • Human nerve growth factor prevents degeneration of basal forebrain cholinergic neurons in primates
    • Koliatsos V.E., Clatterbuck R.E., Nauta H.J., Knusel B., Burton L.E., Hefti F.F., et al. Human nerve growth factor prevents degeneration of basal forebrain cholinergic neurons in primates. Ann Neurol 1991, 30:831-840.
    • (1991) Ann Neurol , vol.30 , pp. 831-840
    • Koliatsos, V.E.1    Clatterbuck, R.E.2    Nauta, H.J.3    Knusel, B.4    Burton, L.E.5    Hefti, F.F.6
  • 9
    • 0037728736 scopus 로고    scopus 로고
    • Passage of vasoactive intestinal peptide across the blood-brain barrier
    • Dogrukol-Ak D., Banks W.A., Tuncel N., Tuncel M. Passage of vasoactive intestinal peptide across the blood-brain barrier. Peptides 2003, 24:437-444.
    • (2003) Peptides , vol.24 , pp. 437-444
    • Dogrukol-Ak, D.1    Banks, W.A.2    Tuncel, N.3    Tuncel, M.4
  • 11
    • 0033401128 scopus 로고    scopus 로고
    • Multiple antioxidants in the prevention and treatment of neurodegenerative disease: analysis of biologic rationale
    • Prasad K.N., Cole W.C., Hovland A.R., Prasad K.C., Nahreini P., Kumar B., et al. Multiple antioxidants in the prevention and treatment of neurodegenerative disease: analysis of biologic rationale. Curr Opin Neurol 1999, 12:761-770.
    • (1999) Curr Opin Neurol , vol.12 , pp. 761-770
    • Prasad, K.N.1    Cole, W.C.2    Hovland, A.R.3    Prasad, K.C.4    Nahreini, P.5    Kumar, B.6
  • 12
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord J.M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 1969, 244:6049-6055.
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 13
    • 4344684255 scopus 로고    scopus 로고
    • Phylogenetic relationships in class I of the superfamily of bacterial, fungal, and plant peroxidases
    • Zamocky M. Phylogenetic relationships in class I of the superfamily of bacterial, fungal, and plant peroxidases. Eur J Biochem 2004, 271:3297-3309.
    • (2004) Eur J Biochem , vol.271 , pp. 3297-3309
    • Zamocky, M.1
  • 14
    • 36448982508 scopus 로고    scopus 로고
    • Superoxide dismutase/catalase mimetics but not MAP kinase inhibitors are neuroprotective against oxygen/glucose deprivation-induced neuronal death in hippocampus
    • Zhou M., Dominguez R., Baudry M. Superoxide dismutase/catalase mimetics but not MAP kinase inhibitors are neuroprotective against oxygen/glucose deprivation-induced neuronal death in hippocampus. JNeurochem 2007, 103:2212-2223.
    • (2007) JNeurochem , vol.103 , pp. 2212-2223
    • Zhou, M.1    Dominguez, R.2    Baudry, M.3
  • 15
    • 0027530638 scopus 로고
    • Effects of tocopherol and deprenyl on the progression of disability in early Parkinson's disease. The Parkinson Study Group
    • Effects of tocopherol and deprenyl on the progression of disability in early Parkinson's disease. The Parkinson Study Group. N Engl J 1993, 328:176-183.
    • (1993) N Engl J , vol.328 , pp. 176-183
  • 16
    • 0029809527 scopus 로고    scopus 로고
    • Alpha-tocopherol in the ventricular cerebrospinal fluid of Parkinson's disease patients: dose-response study and correlations with plasma levels
    • Pappert E.J., Tangney C.C., Goetz C.G., Ling Z.D., Lipton J.W., Stebbins G.T., et al. Alpha-tocopherol in the ventricular cerebrospinal fluid of Parkinson's disease patients: dose-response study and correlations with plasma levels. Neurology 1996, 47:1037-1042.
    • (1996) Neurology , vol.47 , pp. 1037-1042
    • Pappert, E.J.1    Tangney, C.C.2    Goetz, C.G.3    Ling, Z.D.4    Lipton, J.W.5    Stebbins, G.T.6
  • 17
    • 0141927263 scopus 로고    scopus 로고
    • Stealth liposomes and long circulating nanoparticles: critical issues in pharmacokinetics, opsonization and protein-binding properties
    • Moghimi S.M., Szebeni J. Stealth liposomes and long circulating nanoparticles: critical issues in pharmacokinetics, opsonization and protein-binding properties. Prog Lipid Res 2003, 42:463-478.
    • (2003) Prog Lipid Res , vol.42 , pp. 463-478
    • Moghimi, S.M.1    Szebeni, J.2
  • 18
    • 0037141576 scopus 로고    scopus 로고
    • Water-based nanoparticulate polymeric system for protein delivery: permeability control and vaccine application
    • Prokop A., Kozlov E., Newman G.W., Newman M.J. Water-based nanoparticulate polymeric system for protein delivery: permeability control and vaccine application. Biotechnol Bioeng 2002, 78:459-466.
    • (2002) Biotechnol Bioeng , vol.78 , pp. 459-466
    • Prokop, A.1    Kozlov, E.2    Newman, G.W.3    Newman, M.J.4
  • 19
    • 2442686515 scopus 로고    scopus 로고
    • Bioorganic synthesis in reverse micelles and related systems
    • Klyachko N.L., Levashov A.V. Bioorganic synthesis in reverse micelles and related systems. Curr Opin Colloid Int Sci 2003, 8:179-186.
    • (2003) Curr Opin Colloid Int Sci , vol.8 , pp. 179-186
    • Klyachko, N.L.1    Levashov, A.V.2
  • 20
    • 11844291928 scopus 로고    scopus 로고
    • Polymer nanocarriers protecting active enzyme cargo against proteolysis
    • Dziubla T.D., Karim A., Muzykantov V.R. Polymer nanocarriers protecting active enzyme cargo against proteolysis. J Control Release 2005, 102:427-439.
    • (2005) J Control Release , vol.102 , pp. 427-439
    • Dziubla, T.D.1    Karim, A.2    Muzykantov, V.R.3
  • 21
    • 38049049706 scopus 로고    scopus 로고
    • Effect of polymer amphiphilicity on loading of a therapeutic enzyme into protective filamentous and spherical polymer nanocarriers
    • Simone E.A., Dziubla T.D., Colon-Gonzalez F., Discher D.E., Muzykantov V.R. Effect of polymer amphiphilicity on loading of a therapeutic enzyme into protective filamentous and spherical polymer nanocarriers. Biomacromolecules 2007, 8:3914-3921.
    • (2007) Biomacromolecules , vol.8 , pp. 3914-3921
    • Simone, E.A.1    Dziubla, T.D.2    Colon-Gonzalez, F.3    Discher, D.E.4    Muzykantov, V.R.5
  • 23
    • 0032580354 scopus 로고    scopus 로고
    • Drug delivery and targeting
    • Langer R. Drug delivery and targeting. Nature 1998, 392:5-10.
    • (1998) Nature , vol.392 , pp. 5-10
    • Langer, R.1
  • 24
    • 0026639156 scopus 로고
    • Brain and tissue distribution of polyethylene glycol-conjugated superoxide dismutase in rats
    • Yoshida K., Burton G.F., McKinney J.S., Young H., Ellis E.F. Brain and tissue distribution of polyethylene glycol-conjugated superoxide dismutase in rats. Stroke 1992, 23:865-869.
    • (1992) Stroke , vol.23 , pp. 865-869
    • Yoshida, K.1    Burton, G.F.2    McKinney, J.S.3    Young, H.4    Ellis, E.F.5
  • 25
    • 0029398545 scopus 로고
    • Water-soluble block polycations as carriers for olygonucleotide delivery
    • Kabanov A., Vinogradov S., Suzdaltseva Y., Alakhov V. Water-soluble block polycations as carriers for olygonucleotide delivery. Bioconjug Chem 1995, 6:639-643.
    • (1995) Bioconjug Chem , vol.6 , pp. 639-643
    • Kabanov, A.1    Vinogradov, S.2    Suzdaltseva, Y.3    Alakhov, V.4
  • 26
    • 0035858376 scopus 로고    scopus 로고
    • Pronounced activity of enzymes through the incorporation into the core of polyion complex micelles made from charged block copolymers
    • Harada A., Kataoka K. Pronounced activity of enzymes through the incorporation into the core of polyion complex micelles made from charged block copolymers. J Control Release 2001, 72:85-91.
    • (2001) J Control Release , vol.72 , pp. 85-91
    • Harada, A.1    Kataoka, K.2
  • 27
    • 0348110661 scopus 로고    scopus 로고
    • Switching by pulse electric field of the elevated enzymatic reaction in the core of polyion complex micelles
    • Harada A., Kataoka K. Switching by pulse electric field of the elevated enzymatic reaction in the core of polyion complex micelles. J Am Chem Soc 2003, 125:15306-15307.
    • (2003) J Am Chem Soc , vol.125 , pp. 15306-15307
    • Harada, A.1    Kataoka, K.2
  • 29
    • 34648831710 scopus 로고    scopus 로고
    • Self-assembled nano-bioreactor from block ionomers with elevated and stabilized enzymatic function
    • Kawamura A., Harada A., Kono K., Kataoka K. Self-assembled nano-bioreactor from block ionomers with elevated and stabilized enzymatic function. Bioconjug Chem 2007, 18:1555-1559.
    • (2007) Bioconjug Chem , vol.18 , pp. 1555-1559
    • Kawamura, A.1    Harada, A.2    Kono, K.3    Kataoka, K.4
  • 30
    • 0032213191 scopus 로고    scopus 로고
    • Self-assembly of polyamine-poly(ethylene glycol) copolymers with phosphorothioate oligonucleotides
    • Vinogradov S., Bronich T., Kabanov A. Self-assembly of polyamine-poly(ethylene glycol) copolymers with phosphorothioate oligonucleotides. Bioconjug Chem 1998, 9:805-812.
    • (1998) Bioconjug Chem , vol.9 , pp. 805-812
    • Vinogradov, S.1    Bronich, T.2    Kabanov, A.3
  • 31
    • 0040488485 scopus 로고    scopus 로고
    • Recognition of DNA topology in reactions between plasmid DNA and cationic copolymers
    • Bronich T., Nguyen H., Eisenberg A., Kabanov A. Recognition of DNA topology in reactions between plasmid DNA and cationic copolymers. JAm Chem Soc 2000, 122:8339-8343.
    • (2000) JAm Chem Soc , vol.122 , pp. 8339-8343
    • Bronich, T.1    Nguyen, H.2    Eisenberg, A.3    Kabanov, A.4
  • 32
    • 0032875666 scopus 로고    scopus 로고
    • Poly(ethylene glycol)-polyethyleneimine NanoGel (TM) particles: novel drug delivery systems for antisense oligonucleotides colloids and surfaces
    • Vinogradov S., Batrakova E., Kabanov A. Poly(ethylene glycol)-polyethyleneimine NanoGel (TM) particles: novel drug delivery systems for antisense oligonucleotides colloids and surfaces. Colloids Surf. B-Biointerfaces 1999, 16:291-304.
    • (1999) Colloids Surf. B-Biointerfaces , vol.16 , pp. 291-304
    • Vinogradov, S.1    Batrakova, E.2    Kabanov, A.3
  • 33
    • 59749090938 scopus 로고    scopus 로고
    • AFM for analysis of structure and dynamics of DNA and protein-DNA complexes
    • Lyubchenko Y.L., Shlyakhtenko L.S. AFM for analysis of structure and dynamics of DNA and protein-DNA complexes. Methods 2009, 47:206-213.
    • (2009) Methods , vol.47 , pp. 206-213
    • Lyubchenko, Y.L.1    Shlyakhtenko, L.S.2
  • 34
    • 67649099651 scopus 로고    scopus 로고
    • Atomic force microscopy imaging and probing of DNA, proteins, and protein DNA complexes: silatrane surface chemistry
    • Lyubchenko Y.L., Shlyakhtenko L.S., Gall A.A. Atomic force microscopy imaging and probing of DNA, proteins, and protein DNA complexes: silatrane surface chemistry. Methods Mol Biol 2009, 543:337-351.
    • (2009) Methods Mol Biol , vol.543 , pp. 337-351
    • Lyubchenko, Y.L.1    Shlyakhtenko, L.S.2    Gall, A.A.3
  • 35
    • 0037841390 scopus 로고    scopus 로고
    • Silatrane-based surface chemistry for immobilization of DNA, protein-DNA complexes and other biological materials
    • Shlyakhtenko L.S., Gall A.A., Filonov A., Cerovac Z., Lushnikov A., Lyubchenko Y.L. Silatrane-based surface chemistry for immobilization of DNA, protein-DNA complexes and other biological materials. Ultramicroscopy 2003, 97:279-287.
    • (2003) Ultramicroscopy , vol.97 , pp. 279-287
    • Shlyakhtenko, L.S.1    Gall, A.A.2    Filonov, A.3    Cerovac, Z.4    Lushnikov, A.5    Lyubchenko, Y.L.6
  • 36
    • 0035141232 scopus 로고    scopus 로고
    • Pluronic P85 enhances the delivery of digoxin to the brain: in vitro and in vivo studies
    • Batrakova E., Miller D., Li S., Alakhov V., Kabanov A., Elmquist W. Pluronic P85 enhances the delivery of digoxin to the brain: in vitro and in vivo studies. J Pharmacol Exp Ther 2001, 296:551-557.
    • (2001) J Pharmacol Exp Ther , vol.296 , pp. 551-557
    • Batrakova, E.1    Miller, D.2    Li, S.3    Alakhov, V.4    Kabanov, A.5    Elmquist, W.6
  • 37
    • 36249030596 scopus 로고    scopus 로고
    • Permeability of the blood-brain barrier to a novel satiety molecule nesfatin-1
    • Price T.O., Samson W.K., Niehoff M.L., Banks W.A. Permeability of the blood-brain barrier to a novel satiety molecule nesfatin-1. Peptides 2007, 28:2372-2381.
    • (2007) Peptides , vol.28 , pp. 2372-2381
    • Price, T.O.1    Samson, W.K.2    Niehoff, M.L.3    Banks, W.A.4
  • 38
    • 33646511379 scopus 로고    scopus 로고
    • Immobilization of bovine catalase in sol-gels
    • Jurgen-Lohmann D.L., Legge R.L. Immobilization of bovine catalase in sol-gels. Enzyme Microb Tech 2006, 39:626-633.
    • (2006) Enzyme Microb Tech , vol.39 , pp. 626-633
    • Jurgen-Lohmann, D.L.1    Legge, R.L.2
  • 39
    • 0030573881 scopus 로고    scopus 로고
    • Soluble stoichiometric complexes from poly(N-ethyl-4-vinylpyridinium) cations and poly(ethylene oxide)-block-poly(methacrylate) anions
    • Kabanov A., Bronich T., Kabanov V., Yu K., Eisenberg A. Soluble stoichiometric complexes from poly(N-ethyl-4-vinylpyridinium) cations and poly(ethylene oxide)-block-poly(methacrylate) anions. Macromolecules 1996, 29:6797-6802.
    • (1996) Macromolecules , vol.29 , pp. 6797-6802
    • Kabanov, A.1    Bronich, T.2    Kabanov, V.3    Yu, K.4    Eisenberg, A.5
  • 40
    • 51049092308 scopus 로고    scopus 로고
    • Factors affecting the clearance and biodistribution of polymeric nanoparticles
    • Alexis F., Pridgen E., Molnar L.K., Farokhzad O.C. Factors affecting the clearance and biodistribution of polymeric nanoparticles. Mol Pharm 2008, 5:505-515.
    • (2008) Mol Pharm , vol.5 , pp. 505-515
    • Alexis, F.1    Pridgen, E.2    Molnar, L.K.3    Farokhzad, O.C.4
  • 41
    • 66749179382 scopus 로고    scopus 로고
    • Tissue- and organ-selective biodistribution of NIR fluorescent quantum dots
    • Choi H.S., Ipe B.I., Misra P., Lee J.H., Bawendi M.G., Frangioni J.V. Tissue- and organ-selective biodistribution of NIR fluorescent quantum dots. Nano Lett 2009, 9:2354-2359.
    • (2009) Nano Lett , vol.9 , pp. 2354-2359
    • Choi, H.S.1    Ipe, B.I.2    Misra, P.3    Lee, J.H.4    Bawendi, M.G.5    Frangioni, J.V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.