Physiological temperature has a crucial role in amyloid beta in the absence and presence of hydrophobic and hydrophilic nanoparticles

ACS Chemical Neuroscience

Volumn 4, Issue 3, 2013, Pages 375-378

  Ghavami, Mahdi ^a   Rezaei, Meisam ^b   Ejtehadi, Reza ^b   Lotfi, Mina ^c   Shokrgozar, Mohammad A ^a   Abd Emamy, Baharak ^a   Raush, Jens ^d   Mahmoudi, Morteza ^c,e  

^a PASTEUR INSTITUTE OF IRAN   (Iran)

^b SHARIF UNIVERSITY OF TECHNOLOGY   (Iran)

^c TEHRAN UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^d UNIVERSITY COLLEGE DUBLIN   (Ireland)

^e UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

Amyloid beta; fibrillation; hydrophilic NPs; hydrophobic NPs; physiological temperature

Indexed keywords

AMYLOID BETA PROTEIN; NANOPARTICLE; POLYSTYRENE; SILICON DIOXIDE;

ACCELERATION; ARTICLE; BODY TEMPERATURE; DRUG INHIBITION; HUMAN; IN VIVO STUDY; PRIORITY JOURNAL;

AMYLOID BETA-PEPTIDES; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; NANOPARTICLES; PHYSIOLOGICAL PHENOMENA; POLYSTYRENES; SILICON DIOXIDE; TEMPERATURE;

EID: 84875516187     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn300205g     Document Type: Article

References (41)

1. Sipe, J. D. (1992) Amyloidosis Annu. Rev. Biochem. 61, 947-975
2. Serpell, L. C. (2000) Alzheimer's amyloid fibrils: structure and assembly Biochim. Biophys. Acta 1502, 16-30
3. Hardy, J. and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297, 353-356
4. Williams, A. D., Portelius, E., Kheterpal, I., Guo, J., Cook, K. D., Xu, Y., and Wetzel, R. (2004) Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis J. Mol. Biol. 335, 833-842
5. Prusiner, S. B. (1998) Prions Proc. Natl. Acad. Sci. U.S.A. 95, 13363-13383
6. Khurana, R., Ionescu-Zanetti, C., Pope, M., Li, J., Nielson, L., Ramirez-Alvarado, M., Regan, L., Fink, A. L., and Carter, S. A. (2003) A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy Biophys. J. 85, 1135-1144
7. Chen, S., Berthelier, V., Hamilton, J. B. O. N., B., and Wetzel, R. (2002) Amyloid-like features of polyglutamine aggregates and their assembly kinetics Biochemistry 41, 7391-7399
8. Ferkinghoff-Borg, J., Fonslet, J., Andersen, C. B., Krishna, S., Pigolotti, S., Yagi, H., Goto, Y., Otzen, D., and Jensen, M. H. (2010) Stop-and-go kinetics in amyloid fibrillation Phys. Rev. E 82, 010901
9. Naiki, H. (1977) Amyloid Int. J. Exp. Clin. Invest. 4, 223-232
10. McParland, V. J., Kalverda, A. P., Homans, S. W., and Radford, S. E. (2002) Structural properties of an amyloid precursor ofβ2-microglobulin Nat. Struct. Biol. 9, 326-331
11. Chiti, F. and Dobson, C. M. (2006) Protein Misfolding, Functional Amyloid, and Human Disease Annu. Rev. Biochem. 75, 333-366
12. Campioni, S., Mannini, B., Zampagni, M., Pensalfini, A., Parrini, C., Evangelisti, E., Relini, A., Stefani, M., Dobson, C. M., Cecchi, C., and Chiti, F. (2010) A causative link between the structure of aberrant protein oligomers and their toxicity Nat. Chem. Biol. 6, 140-147
13. Fei, L. and Perrett, S. (2009) Int. J. Mol. Sci. 10, 646
14. Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Margaret, M., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., and Teplow, D. B. (1999) Amyloid β-Protein Fibrillogenesis J. Biol. Chem. 274, 25945-25952
15. Nelson, R. and Eisenberg, D. (2006) Structural models of amyloid-like fibrils Adv. Protein Chem. 73, 235-282
16. Sato, T., Kienlen-Campard, P., Ahmed, M., Liu, W., Li, H., Elliott, J. I., Aimoto, S., Constantinescu, S. N., Octave, J. N., and Smith, S. O. (2006) Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42 Biochemistry 45, 5503-5516
17. Petkova, A. T., Yau, W. M., and Tycko, R. (2006) Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils Biochemistry 45, 498-512
18. Linse, S., Cabaleiro-Lago, C., Xue, W.-F., Lynch, I., Lindman, S., Thulin, E., Radford, S. E., and Dawson, K. A. (2007) Nucleation of protein fibrillation by nanoparticles Proc. Natl. Acad. Sci. U.S.A. 104, 8691-8696
19. Cabaleiro-Lago, C., Quinlan-Pluck, F., Lynch, I., Lindman, S., Minogue, A. M., Thulin, E., Walsh, D. M., Dawson, K. A., and Linse, S. (2008) Inhibition of Amyloid β Protein Fibrillation by Polymeric Nanoparticles J. Am. Chem. Soc. 130, 15437-15443
20. Cabaleiro-Lago, C., Lynch, I., Dawson, K. A., and Linse, S. (2009) Inhibition of IAPP and IAPP(20-29) Fibrillation by Polymeric Nanoparticles Langmuir 26, 3453-3461
21. Mahmoudi, M., Lynch, I., Ejtehadi, M. R., Monopoli, M. P., Bombelli, F. B., and Laurent, S. (2011) Protein-Nanoparticle Interactions: Opportunities and Challenges Chem. Rev. 111, 5610-5637
22. Mahmoudi, M., Akhavan, O., Ghavami, M., Rezaee, F., and Ghiasi, S. M. A. (2012) Graphene oxide strongly inhibits amyloid beta fibrillation Nanoscale 4, 7322-7325
23. Sabaté, R., Gallardo, M., and Estelrich, J. (2005) Temperature dependence of the nucleation constant rate in β amyloid fibrillogenesis Int. J. Biol. Macromol. 35, 9-13
24. Gursky, O. and Aleshkov, S. (2000) Temperature-dependent β-sheet formation in β-amyloid Aβ1-40 peptide in water: uncoupling β-structure folding from aggregation Biochim. Biophys. Acta 1476, 93-102
25. Shehi, E., Fusi, P., Secundo, F., Pozzuolo, S., Bairati, A., and Tortora, P. (2003) Temperature-Dependent, Irreversible Formation of Amyloid Fibrils by a Soluble Human Ataxin-3 Carrying a Moderately Expanded Polyglutamine Stretch (Q36) Biochemistry 42, 14626-14632
26. Chu, H.-L. and Lin, S.-Y. (2001) Temperature-induced conformational changes in amyloid β(1-40) peptide investigated by simultaneous FT-IR microspectroscopy with thermal system Biophys. Chem. 89, 173-180
27. Krol, S., Macrez, R., Docagne, F., Defer, G., Laurent, S., Rahman, M., Hajipour, M. J., Kehoe, P. G., and Mahmoudi, M. (2012) Therapeutic Benefits from Nanoparticles: The Potential Significance of Nanoscience in Diseases with Compromise to the Blood Brain Barrier. Chem. Rev. published online Nov 19, 2012. DOI: 10.1021/cr200472g.
28. Ishigaki, D., Ogasawara, K., Yoshioka, Y., Chida, K., Sasaki, M., Fujiwara, S., Aso, K., Kobayashi, M., Yoshida, K., Terasaki, K., Inoue, T., and Ogawa, A. (2009) Brain Temperature Measured Using Proton MR Spectroscopy Detects Cerebral Hemodynamic Impairment in Patients With Unilateral Chronic Major Cerebral Artery Steno-Occlusive Disease Stroke 40, 3012-3016
29. Colbourne, F., Nurse, S. M., and Corbett, D. (1993) Temperature changes associated with forebrain ischemia in the gerbil Brain Res. 602, 264-267
30. Sukstanskii, A. L. and Yablonskiy, D. A. (2006) Theoretical model of temperature regulation in the brain during changes in functional activity Proc. Natl. Acad. Sci. U.S.A. 103, 12144-12149
31. Corbett, R., Laptook, A., and Weatherall, P. (1997) Noninvasive Measurements of Human Brain Temperature Using Volume-Localized Proton Magnetic Resonance Spectroscopy J. Cereb. Blood Flow Metab. 17, 363-369
32. Collins, C. M., Smith, M. B., and Turner, R. (2004) Model of local temperature changes in brain upon functional activation J. Appl. Physiol. 97, 2051-2055
33. Hasday, J. D. and Singh, I. S. (2000) Fever and the heat shock response: distinct, partially overlapping processes Cell Stress Chaperones 5, 471-480
34. Fei, L. and Perrett, S. (2009) Effect of Nanoparticles on Protein Folding and Fibrillogenesis Int. J. Mol. Sci. 10, 646-655
35. Ikeda, K., Okada, T., Sawada, S.-i., Akiyoshi, K., and Matsuzaki, K. (2006) Inhibition of the formation of amyloid β-protein fibrils using biocompatible nanogels as artificial chaperones FEBS Lett. 580, 6587-6595
36. Skaat, H., Shafir, G., and Margel, S. (2011) Acceleration and inhibition of amyloid-β fibril formation by peptide-conjugated fluorescent-maghemite nanoparticles J. Nanoparticle Res. 13, 3521-3534
37. Kogan, M. J., Bastus, N. G., Amigo, R., Grillo-Bosch, D., Araya, E., Turiel, A., Labarta, A., Giralt, E., and Puntes, V. F. (2005) Nanoparticle-Mediated Local and Remote Manipulation of Protein Aggregation Nano Lett. 6, 110-115
38. Laurent, S., Ejtehadi, M. R., Rezaei, M., Kehoe, P. G., and Mahmoudi, M. (2012) Interdisciplinary challenges and promising theranostic effects of nanoscience in Alzheimer's disease RSC Adv. 2, 5008-5033
39. Monopoli, M. P., Walczyk, D., Campbell, A., Elia, G., Lynch, I., Baldelli Bombelli, F., and Dawson, K. A. (2011) Physical-Chemical Aspects of Protein Corona: Relevance to in Vitro and in Vivo Biological Impacts of Nanoparticles J. Am. Chem. Soc. 133, 2525-2534
40. Walczyk, D., Bombelli, F. B., Monopoli, M. P., Lynch, I., and Dawson, K. A. (2010) What the Cell "Sees" in Bionanoscience J. Am. Chem. Soc. 132, 5761-5768
41. Cedervall, T., Lynch, I., Foy, M., BerggaÌŠrd, T., Donnelly, S. C., Cagney, G., Linse, S., and Dawson, K. A. (2007) Detailed Identification of Plasma Proteins Adsorbed on Copolymer Nanoparticles Angew. Chem., Int. Ed. 119, 5856-5858