Nanomedicine for prion disease treatment: New insights into the role of dendrimers

Prion

Volumn 7, Issue 3, 2013, Pages 198-202

  McCarthy, James M ^a   Appelhans, Dietmar ^b   Tatzelt, Jörg ^c,d   Rogers, Mark S ^a  

^a UNIVERSITY COLLEGE DUBLIN   (Ireland)

^b LEIBNIZ INSTITUTE OF POLYMER RESEARCH DRESDEN   (Germany)

^c UNIVERSITY OF MUNICH   (Germany)

^d GERMAN CENTER FOR NEURODEGENERATIVE DISEASES DZNE   (Germany)

Author keywords

Amyloid; Dendrimer; Nanomedicine; Neurodegeneration; Prion; PrP N terminal; Scrapie cell assay; Therapeutic

Indexed keywords

CHLOROQUINE; DENDRIMER; MALTOSE POLY(PROPYLENE IMINE) GENERATION FIVE; UNCLASSIFIED DRUG;

ARTICLE; BIOGENESIS; BRAIN HOMOGENATE; CELL CULTURE; CELL DENSITY; CELL STRUCTURE; CHEMICAL INTERACTION; CHEMICAL STRUCTURE; CONCENTRATION RESPONSE; CONFOCAL MICROSCOPY; DEGENERATIVE DISEASE; DRUG EFFICACY; ENZYME LINKED IMMUNOSPOT ASSAY; GENETIC TRANSFECTION; HUMAN; IN VITRO STUDY; INTRACELLULAR SIGNALING; LYSOSOME; MOLECULE; NANOMEDICINE; NONHUMAN; PRION DISEASE; PROTEIN CLEAVAGE;

AMYLOID; DENDRIMER; NANOMEDICINE; NEURODEGENERATION; PRION; PRP N-TERMINAL; SCRAPIE CELL ASSAY; THERAPEUTIC;

ANIMALS; DENDRIMERS; HUMANS; NANOMEDICINE; PRION DISEASES; PRIONS; PROTEIN CONFORMATION;

ANIMALIA;

EID: 84879813285     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.24431     Document Type: Article

References (29)

1. Supattapone S, Nguyen HO, Cohen FE, Prusiner SB, Scott MR. Elimination of prions by branched polyamines and implications for therapeutics. Proc Natl Acad Sci U S A 1999; 96:14529-34; PMID:10588739; http://dx.doi.org/10.1073/pnas.96. 25.14529.
2. 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 2008; 14:7030-41; PMID:18576443; http://dx.doi.org/10.1002/chem.200800342.
3. Fischer M, Appelhans D, Schwarz S, Klajnert B, Bryszewska M, Voit B, et al. Influence of surface functionality of poly(propylene imine) dendrimers on protease resistance and propagation of the scrapie prion protein. Biomacromolecules 2010; 11:1314-25; PMID:20405854; http://dx.doi.org/10.1021/ bm100101s.
4. Supattapone S, Wille H, Uyechi L, Safar J, Tremblay P, Szoka FC, et al. Branched polyamines cure prioninfected neuroblastoma cells. J Virol 2001; 75:3453-61; PMID:11238871; http://dx.doi.org/10.1128/JVI.75.7.3453-3461.2001.
5. Solassol J, Crozet C, Perrier V, Leclaire J, Béranger F, Caminade AM, et al. Cationic phosphorus-containing dendrimers reduce prion replication both in cell culture and in mice infected with scrapie. J Gen Virol 2004; 85:1791-9; PMID:15166465; http://dx.doi.org/10.1099/vir.0.19726-0.
6. Sebestik J, Niederhafner P, Jezek J. Peptide and glycopeptide dendrimers and analogous dendrimeric structures and their biomedical applications. Amino Acids 2011; 40:301-70; PMID:21058024; http://dx.doi.org/10.1007/s00726-010-0707- z.
7. McCarthy JM, Rasines Moreno B, Filippini D, Komber H, Maly M, Cernescu M, et al. Influence of surface groups on poly(propylene imine) dendrimers antiprion activity. Biomacromolecules 2013; 14:27-37; PMID:23234313; http://dx.doi.org/10.1021/bm301165u.
8. Ciolkowski M, Pałecz B, Appelhans D, Voit B, Klajnert B, Bryszewska M. The influence of maltose modified poly(propylene imine) dendrimers on hen egg white lysozyme structure and thermal stability. Colloids Surf B Biointerfaces 2012; 95:103-8; PMID:22410344; http://dx.doi.org/10.1016/j. colsurfb.2012.02.021.
9. Boas U, Christensen JB, Heegaard PMH. Dendrimers in medicine and biotechnology: new molecular tools. Cambridge, U.K.: Royal Society of Chemistry, 2006.
10. McCarthy JM, Franke M, Resenberger UK, Waldron S, Simpson JC, Tatzelt J, et al. Anti-prion drug mPPIg5 inhibits PrP(C) conversion to PrP(Sc). PLoS One 2013; 8:e55282; PMID:23383136; http://dx.doi.org/10.1371/journal.pone.0055282.
11. Klöhn PC, Stoltze L, Flechsig E, Enari M, Weissmann C. A quantitative, highly sensitive cell-based infectivity assay for mouse scrapie prions. Proc Natl Acad Sci U S A 2003; 100:11666-71; PMID:14504404; http://dx.doi.org/10.1073/pnas.1834432100.
12. Pless DD, Wellner RB. In vitro fusion of endocytic vesicles: effects of reagents that alter endosomal pH. J Cell Biochem 1996; 62:27-39; PMID:8836873; http://dx.doi.org/10.1002/(SICI)1097-4644(199607)62:1<27::AID-JCB4>3.0. CO;2-3.
13. McCarthy JM, Rasines B, Appelhans D, Rogers M. Differentiating prion strains using dendrimers. Adv Healthc Mater 2012; 1:768-72; PMID:23184829; http://dx.doi.org/10.1002/adhm.201200151.
14. Lim YB, Mays CE, Kim Y, Titlow WB, Ryou C. The inhibition of prions through blocking prion conversion by permanently charged branched polyamines of low cytotoxicity. Biomaterials 2010; 31:2025-33; PMID:20022103; http://dx.doi.org/10.1016/j.biomaterials.2009.11.085.
15. Caughey B, Raymond GJ, Ernst D, Race RE. N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state. J Virol 1991; 65:6597-603; PMID:1682507.
16. Deleault NR, Kascsak R, Geoghegan JC, Supattapone S. Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro. Biochemistry 2010; 49:3928-34; PMID:20377181; http://dx.doi.org/10.1021/bi100370b.
17. Heegaard PMH, Pedersen HG, Flink J, Boas U. Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers. FEBS Lett 2004; 577:127-33; PMID:15527773; http://dx.doi.org/10. 1016/j.febslet.2004.09.073.
18. Klajnert B, Cortijo-Arellano M, Cladera J, Bryszewska M. Influence of dendrimer's structure on its activity against amyloid fibril formation. Biochem Biophys Res Commun 2006; 345:21-8; PMID:16674918; http://dx.doi.org/10.1016/j. bbrc.2006.04.041.
19. Klajnert B, Cortijo-Arellano M, Cladera J, Majoral JP, Caminade AM, Bryszewska M. Influence of phosphorus dendrimers on the aggregation of the prion peptide PrP 185-208. Biochem Biophys Res Commun 2007; 364:20-5; PMID:17927954; http://dx.doi.org/10.1016/j.bbrc.2007.09.083.
20. Colby DW, Prusiner SB. Prions. Cold Spring Harb Perspect Biol 2011; 3:a006833; PMID:21421910; http://dx.doi.org/10.1101/cshperspect.a006833.
21. Barry AE, Klyubin I, Mc Donald JM, Mably AJ, Farrell MA, Scott M, et al. Alzheimer's disease brain-derived amyloid-β-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein. J Neurosci 2011; 31:7259-63; PMID:21593310; http://dx.doi.org/10.1523/JNEUROSCI.6500-10.2011.
22. Resenberger UK, Harmeier A, Woerner AC, Goodman JL, Müller V, Krishnan R, et al. The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication. EMBO J 2011; 30:2057-70; PMID:21441896; http://dx.doi.org/10.1038/emboj.2011.86.
23. Soto C. Prion hypothesis: the end of the controversy? Trends Biochem Sci 2011; 36:151-8; PMID:21130657; http://dx.doi.org/10.1016/j.tibs.2010.11.001.
24. Lane AR, Stanley CJ, Wilson SM. Binding of pathological forms of prion proteins. MICROSENS BIOPHAGE LTD (GB), 2010.
25. Klajnert B, Cladera J, Bryszewska M. Molecular interactions of dendrimers with amyloid peptides: pH dependence. Biomacromolecules 2006; 7:2186-91; PMID:16827586; http://dx.doi.org/10.1021/bm060229s.
26. Klajnert B, Cangiotti M, Calici S, Majoral JP, Caminade AM, Cladera J, et al. EPR study of the interactions between dendrimers and peptides involved in Alzheimer's and prion diseases. Macromol Biosci 2007; 7:1065-74; PMID:17654761; http://dx.doi.org/10.1002/mabi.200700049.
27. Wasiak T, Ionov M, Nieznanski K, Nieznanska H, Klementieva O, Granell M, et al. Phosphorus Dendrimers Affect Alzheimer's (Aβ1-28) Peptide and MAP-Tau Protein Aggregation. Mol Pharm 2011; 9:458-69; http://dx.doi.org/10. 1021/mp2005627.
28. Lee VM, Goedert M, Trojanowski JQ. Neurodegenerative tauopathies. Annu Rev Neurosci 2001; 24:1121-59; PMID:11520930; http://dx.doi.org/10.1146/annurev. neuro.24.1.1121.
29. Janaszewska A, Ziemba B, Ciepluch K, Appelhans D, Voit B, Klajnert B, et al. The biodistribution of maltotriose modified poly (propylene imine)(PPI) dendrimers conjugated with fluorescein-proofs of crossing blood-brain-barrier. New J Chem 2012; 36:350-3; http://dx.doi.org/10.1039/c1nj20444k.