메뉴 건너뛰기




Volumn 31, Issue 8, 2010, Pages 2025-2033

The inhibition of prions through blocking prion conversion by permanently charged branched polyamines of low cytotoxicity

Author keywords

Branched polyamines; Cytotoxicity; Prion; Prion protein conversion; Quaternization; Therapy

Indexed keywords

ACIDIC PH; ACTION MECHANISMS; ANTI-PRION AGENTS; BRANCHED POLYAMINES; IN-VITRO; INFECTED CELLS; ISOFORMS; NEUROBLASTOMA CELLS; NONTOXIC CONCENTRATIONS; POLYAMIDOAMINE DENDRIMERS; POLYAMINES; POLYETHYLENEIMINE; PRION DISEASE; PRION PROPAGATION; PRION PROTEIN; QUATERNIZATION; STRUCTURAL CONTROL;

EID: 74449085875     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2009.11.085     Document Type: Article
Times cited : (49)

References (36)
  • 2
    • 17444423617 scopus 로고    scopus 로고
    • The public health impact of prion diseases
    • Belay E.D., and Schonberger L.B. The public health impact of prion diseases. Annu Rev Public Health 26 1 (2005) 191-212
    • (2005) Annu Rev Public Health , vol.26 , Issue.1 , pp. 191-212
    • Belay, E.D.1    Schonberger, L.B.2
  • 3
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 216 (1982) 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 4
    • 0002181235 scopus 로고    scopus 로고
    • An introduction to prion biology and diseases
    • Prusiner S.B. (Ed), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Prusiner S.B. An introduction to prion biology and diseases. In: Prusiner S.B. (Ed). Prion biology and diseases. 2nd ed. (2004), Cold Spring Harbor Laboratory Press, Cold Spring Harbor 1-87
    • (2004) Prion biology and diseases. 2nd ed. , pp. 1-87
    • Prusiner, S.B.1
  • 5
    • 3442879322 scopus 로고    scopus 로고
    • Development of the prion concept
    • Prusiner S.B. (Ed), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Prusiner S.B. Development of the prion concept. In: Prusiner S.B. (Ed). Prion biology and diseases. 2nd ed. (2004), Cold Spring Harbor Laboratory Press, Cold Spring Harbor 89-141
    • (2004) Prion biology and diseases. 2nd ed. , pp. 89-141
    • Prusiner, S.B.1
  • 8
    • 2942672631 scopus 로고    scopus 로고
    • Cationic phosphorus-containing dendrimers reduce prion replication both in cell culture and in mice infected with scrapie
    • Solassol J., Crozet C., Perrier V., Leclaire J., Beranger F., Caminade A.-M., et al. Cationic phosphorus-containing dendrimers reduce prion replication both in cell culture and in mice infected with scrapie. J Gen Virol 85 6 (2004) 1791-1799
    • (2004) J Gen Virol , vol.85 , Issue.6 , pp. 1791-1799
    • Solassol, J.1    Crozet, C.2    Perrier, V.3    Leclaire, J.4    Beranger, F.5    Caminade, A.-M.6
  • 9
    • 36649016409 scopus 로고    scopus 로고
    • Guanidino- and urea-modified dendrimers as potent solubilizers of misfolded prion protein aggregates under non-cytotoxic conditions: dependence on dendrimer generation and surface charge
    • Cordes H., Boas U., Olsen P., and Heegaard P.M.H. Guanidino- and urea-modified dendrimers as potent solubilizers of misfolded prion protein aggregates under non-cytotoxic conditions: dependence on dendrimer generation and surface charge. Biomacromolecules 8 11 (2007) 3578-3583
    • (2007) Biomacromolecules , vol.8 , Issue.11 , pp. 3578-3583
    • Cordes, H.1    Boas, U.2    Olsen, P.3    Heegaard, P.M.H.4
  • 10
    • 7544239102 scopus 로고    scopus 로고
    • Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers
    • Heegaard P.M.H., Pedersen H.G., Flink J., and Boas U. Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers. FEBS Lett 577 1-2 (2004) 127-133
    • (2004) FEBS Lett , vol.577 , Issue.1-2 , pp. 127-133
    • Heegaard, P.M.H.1    Pedersen, H.G.2    Flink, J.3    Boas, U.4
  • 11
    • 28444448086 scopus 로고    scopus 로고
    • Influence of heparin and dendrimers on the aggregation of two amyloid peptides related to Alzheimer's and prion diseases
    • Klajnert B., Cortijo-Arellano M., Bryszewska M., and Cladera J. Influence of heparin and dendrimers on the aggregation of two amyloid peptides related to Alzheimer's and prion diseases. Biochem Biophys Res Commun 339 2 (2006) 577-582
    • (2006) Biochem Biophys Res Commun , vol.339 , Issue.2 , pp. 577-582
    • Klajnert, B.1    Cortijo-Arellano, M.2    Bryszewska, M.3    Cladera, J.4
  • 12
  • 13
    • 34548130742 scopus 로고    scopus 로고
    • EPR Study of the interactions between dendrimers and peptides involved in Alzheimer's and prion diseases
    • Klajnert B., Cangiotti M., Calici S., Majoral J.P., Caminade A.M., Cladera J., et al. EPR Study of the interactions between dendrimers and peptides involved in Alzheimer's and prion diseases. Macromol Biosci 7 8 (2007) 1065-1074
    • (2007) Macromol Biosci , vol.7 , Issue.8 , pp. 1065-1074
    • Klajnert, B.1    Cangiotti, M.2    Calici, S.3    Majoral, J.P.4    Caminade, A.M.5    Cladera, J.6
  • 14
    • 34548133091 scopus 로고    scopus 로고
    • Dendrimer effects on peptide and protein fibrillation
    • Heegaard P.M.H., Boas U., and Otzen D.E. Dendrimer effects on peptide and protein fibrillation. Macromol Biosci 7 8 (2007) 1047-1059
    • (2007) Macromol Biosci , vol.7 , Issue.8 , pp. 1047-1059
    • Heegaard, P.M.H.1    Boas, U.2    Otzen, D.E.3
  • 15
    • 33746275959 scopus 로고    scopus 로고
    • Molecular interactions of dendrimers with amyloid peptides: pH dependence
    • Klajnert B., Cladera J., and Bryszewska M. Molecular interactions of dendrimers with amyloid peptides: pH dependence. Biomacromolecules 7 7 (2006) 2186-2191
    • (2006) Biomacromolecules , vol.7 , Issue.7 , pp. 2186-2191
    • Klajnert, B.1    Cladera, J.2    Bryszewska, M.3
  • 17
    • 53849139796 scopus 로고    scopus 로고
    • The influence of densely organized maltose shells on the biological properties of poly(propylene imine) dendrimers: new effects dependent on hydrogen bonding
    • Klajnert B., Appelhans D., Komber H., Morgner N., Schwarz S., Richter S., et al. The influence of densely organized maltose shells on the biological properties of poly(propylene imine) dendrimers: new effects dependent on hydrogen bonding. Chemistry 14 23 (2008) 7030-7041
    • (2008) Chemistry , vol.14 , Issue.23 , pp. 7030-7041
    • Klajnert, B.1    Appelhans, D.2    Komber, H.3    Morgner, N.4    Schwarz, S.5    Richter, S.6
  • 18
    • 0034513037 scopus 로고    scopus 로고
    • Effect of protonation and PAMAM dendrimer size on the complexation and dynamic mobility of 2-naphthol
    • Kleinman M.H., Flory J.H., Tomalia D.A., and Turro N.J. Effect of protonation and PAMAM dendrimer size on the complexation and dynamic mobility of 2-naphthol. J Phys Chem B 104 48 (2000) 11472-11479
    • (2000) J Phys Chem B , vol.104 , Issue.48 , pp. 11472-11479
    • Kleinman, M.H.1    Flory, J.H.2    Tomalia, D.A.3    Turro, N.J.4
  • 19
    • 0034806937 scopus 로고    scopus 로고
    • Cationic hyperbranched poly(amino ester): a novel class of DNA condensing molecule with cationic surface, biodegradable three-dimensional structure, and tertiary amine groups in the interior
    • Lim Y.-b., Kim S.-M., Lee Y., Lee W.-k., Yang T.-g., Lee M.-j., et al. Cationic hyperbranched poly(amino ester): a novel class of DNA condensing molecule with cationic surface, biodegradable three-dimensional structure, and tertiary amine groups in the interior. J Am Chem Soc 123 10 (2001) 2460-2461
    • (2001) J Am Chem Soc , vol.123 , Issue.10 , pp. 2460-2461
    • Lim, Y.-b.1    Kim, S.-M.2    Lee, Y.3    Lee, W.-k.4    Yang, T.-g.5    Lee, M.-j.6
  • 20
    • 20144381403 scopus 로고    scopus 로고
    • Synthesis and characterization of new permanently charged poly(amidoammonium) salts and evaluation of their DNA complexes for gene transport
    • Vuillaume P.Y., Brunelle M., Van Calsteren M.-R., Laurent-Lewandowski S., Begin A., Lewandowski R., et al. Synthesis and characterization of new permanently charged poly(amidoammonium) salts and evaluation of their DNA complexes for gene transport. Biomacromolecules 6 3 (2005) 1769-1781
    • (2005) Biomacromolecules , vol.6 , Issue.3 , pp. 1769-1781
    • Vuillaume, P.Y.1    Brunelle, M.2    Van Calsteren, M.-R.3    Laurent-Lewandowski, S.4    Begin, A.5    Lewandowski, R.6
  • 21
    • 0344494597 scopus 로고    scopus 로고
    • Polyplexes assembled with internally quaternized PAMAM-OH dendrimer and plasmid DNA have a neutral surface and gene delivery potency
    • Lee J.H., Lim Y.-b., Choi J.S., Lee Y., Kim T.-i., Kim H.J., et al. Polyplexes assembled with internally quaternized PAMAM-OH dendrimer and plasmid DNA have a neutral surface and gene delivery potency. Bioconjug Chem 14 6 (2003) 1214-1221
    • (2003) Bioconjug Chem , vol.14 , Issue.6 , pp. 1214-1221
    • Lee, J.H.1    Lim, Y.-b.2    Choi, J.S.3    Lee, Y.4    Kim, T.-i.5    Kim, H.J.6
  • 22
    • 1842609794 scopus 로고    scopus 로고
    • PEI-based vesicle-polymer hybrid gene delivery system with improved biocompatibility
    • Brownlie A., Uchegbu I.F., and Schätzlein A.G. PEI-based vesicle-polymer hybrid gene delivery system with improved biocompatibility. Int J Pharm 274 1-2 (2004) 41-52
    • (2004) Int J Pharm , vol.274 , Issue.1-2 , pp. 41-52
    • Brownlie, A.1    Uchegbu, I.F.2    Schätzlein, A.G.3
  • 24
    • 43049102451 scopus 로고    scopus 로고
    • CRBL cells: establishment, characterization and susceptibility to prion infection
    • Mays C.E., Kang H.-E., Kim Y., Shim S.H., Bang J.-E., Woo H.-J., et al. CRBL cells: establishment, characterization and susceptibility to prion infection. Brain Res 1208 (2008) 170-180
    • (2008) Brain Res , vol.1208 , pp. 170-180
    • Mays, C.E.1    Kang, H.-E.2    Kim, Y.3    Shim, S.H.4    Bang, J.-E.5    Woo, H.-J.6
  • 26
    • 0035086136 scopus 로고    scopus 로고
    • Strain-specified relative conformational stability of the scrapie prion protein
    • Peretz D., Scott M., Groth D., Williamson A., Burton D., Cohen F.E., et al. Strain-specified relative conformational stability of the scrapie prion protein. Protein Sci 10 (2001) 854-863
    • (2001) Protein Sci , vol.10 , pp. 854-863
    • Peretz, D.1    Scott, M.2    Groth, D.3    Williamson, A.4    Burton, D.5    Cohen, F.E.6
  • 27
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • Saborio G.P., Permanne B., and Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411 (2001) 810-813
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 28
    • 69249235730 scopus 로고    scopus 로고
    • Enhancement of protein misfolding cyclic amplification by using concentrated cellular prion protein source
    • Mays C.E., Titlow W., Seward T., Telling G.C., and Ryou C. Enhancement of protein misfolding cyclic amplification by using concentrated cellular prion protein source. Biochem Biophys Res Commun 388 2 (2009) 306-310
    • (2009) Biochem Biophys Res Commun , vol.388 , Issue.2 , pp. 306-310
    • Mays, C.E.1    Titlow, W.2    Seward, T.3    Telling, G.C.4    Ryou, C.5
  • 29
    • 4644335136 scopus 로고    scopus 로고
    • Enhanced transfection efficiency of PAMAM dendrimer by surface modification with l-arginine
    • Choi J.S., Nam K., Park J.-y., Kim J.-B., Lee J.-K., and Park J.-s. Enhanced transfection efficiency of PAMAM dendrimer by surface modification with l-arginine. J Control Release 99 3 (2004) 445-456
    • (2004) J Control Release , vol.99 , Issue.3 , pp. 445-456
    • Choi, J.S.1    Nam, K.2    Park, J.-y.3    Kim, J.-B.4    Lee, J.-K.5    Park, J.-s.6
  • 30
    • 0025304678 scopus 로고
    • Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells
    • Borchelt D.R., Scott M., Taraboulos A., Stahl N., and Prusiner S.B. Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells. J Cell Biol 110 (1990) 743-752
    • (1990) J Cell Biol , vol.110 , pp. 743-752
    • Borchelt, D.R.1    Scott, M.2    Taraboulos, A.3    Stahl, N.4    Prusiner, S.B.5
  • 32
    • 70349466505 scopus 로고    scopus 로고
    • Utility of RNAi-mediated prnp gene silencing in neuroblastoma cells permanently infected by prions: potentials and limitations
    • Kim Y., Han B., Titlow W., Mays C.E., Kwon M., and Ryou C. Utility of RNAi-mediated prnp gene silencing in neuroblastoma cells permanently infected by prions: potentials and limitations. Antiviral Res 84 (2009) 185-193
    • (2009) Antiviral Res , vol.84 , pp. 185-193
    • Kim, Y.1    Han, B.2    Titlow, W.3    Mays, C.E.4    Kwon, M.5    Ryou, C.6
  • 33
    • 0036000144 scopus 로고    scopus 로고
    • Aliphatic ionenes as gene delivery agents: elucidation of structure-function relationship through modification of charge density and polymer length
    • Zelikin A.N., Putnam D., Shastri P., Langer R., and Izumrudov V.A. Aliphatic ionenes as gene delivery agents: elucidation of structure-function relationship through modification of charge density and polymer length. Bioconjug Chem 13 3 (2002) 548-553
    • (2002) Bioconjug Chem , vol.13 , Issue.3 , pp. 548-553
    • Zelikin, A.N.1    Putnam, D.2    Shastri, P.3    Langer, R.4    Izumrudov, V.A.5
  • 34
    • 0001196942 scopus 로고
    • Colloid titration behavior of poly(ethyleneimine)
    • Kokufuta E. Colloid titration behavior of poly(ethyleneimine). Macromolecules 12 2 (1979) 350-351
    • (1979) Macromolecules , vol.12 , Issue.2 , pp. 350-351
    • Kokufuta, E.1
  • 35
    • 23944464631 scopus 로고    scopus 로고
    • Recent advances in rational gene transfer vector design based on poly(ethylene imine) and its derivatives
    • Neu M., Fischer D., and Kissel T. Recent advances in rational gene transfer vector design based on poly(ethylene imine) and its derivatives. J Gene Med 7 8 (2005) 992-1009
    • (2005) J Gene Med , vol.7 , Issue.8 , pp. 992-1009
    • Neu, M.1    Fischer, D.2    Kissel, T.3
  • 36
    • 44849085552 scopus 로고    scopus 로고
    • Dendrimers destabilize proteins in a generation-dependent manner involving electrostatic interactions
    • Giehm L., Christensen C., Boas U., Heegaard P.M.H., and Otzen D.E. Dendrimers destabilize proteins in a generation-dependent manner involving electrostatic interactions. Biopolymers 89 6 (2008) 522-529
    • (2008) Biopolymers , vol.89 , Issue.6 , pp. 522-529
    • Giehm, L.1    Christensen, C.2    Boas, U.3    Heegaard, P.M.H.4    Otzen, D.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.