Interactions between gold nanoparticles and amyloid β 25–35 peptide
- Author(s): Jian Peng 1 ; Jian Weng 1 ; Lei Ren 1 ; Li-Ping Sun 1
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Affiliations:
1:
Department of Biomaterials, College of Materials, Xiamen University, Xiamen 361005, People's Republic of China
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Affiliations:
1:
Department of Biomaterials, College of Materials, Xiamen University, Xiamen 361005, People's Republic of China
- Source:
Volume 8, Issue 4,
December 2014,
p.
295 – 303
DOI: 10.1049/iet-nbt.2013.0071 , Print ISSN 1751-8741, Online ISSN 1751-875X
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Amyloid β 25–35 (Aβ 25–35) peptide is a peculiar peptide for its rapid aggregation properties and high neurotoxicity in Alzheimer's disease. Here, the interactions between gold nanoparticles (GNPs) and Aβ 25–35 monomers, oligomers and fibrils are explored under different molar ratio, temperature and pH by ultraviolet–visible and circular dichroism spectra, thioflavin T fluorescence assay and transmission electron microscope. It is concluded that Aβ 25–35 can induce the aggregation of GNPs at certain concentration of Aβ 25–35 monomer or oligomer. But at higher concentration of Aβ 25–35, GNPs aggregates dissociate again. Furthermore, the aggregation rate increases at higher temperature or for lower pH. These results might provide the basis of a simple diagnostic tool for detecting Alzheimer's disease.
Inspec keywords: molecular biophysics; biochemistry; fluorescence; pH; nanomedicine; diseases; ultraviolet spectra; transmission electron microscopy; patient diagnosis; circular dichroism; visible spectra; gold; nanoparticles; proteins; dissociation
Other keywords: pH; circular dichroism spectra; amyloid β25-35 peptide; dissociation; ultraviolet-visible spectra; gold nanoparticles; Aβ25−35 oligomers; Aβ25−35 fibrils; diagnostic tool; neurotoxicity; transmission electron microscope; aggregation; Au; Alzheimer's disease detection; molar ratio; Aβ25−35 monomers; thioflavin T fluorescence assay
Subjects: Physical chemistry of biomolecular solutions and condensed states; Patient diagnostic methods and instrumentation; Decomposition reactions (pyrolysis, dissociation, and group ejection); Biomolecular interactions, charge transfer complexes; Electrochemistry and electrophoresis; Electronic structure and spectra of macromolecules; Interactions with radiations at the biomolecular level; Nanotechnology applications in biomedicine
References
-
-
1)
-
35. Biancalana, M., Koide, S.: ‘Molecular mechanism of Thioflavin-T binding to amyloid fibrils’, Biochim. Biophys. Acta, 2010, 1804, pp. 1405–1412 (doi: 10.1016/j.bbapap.2010.04.001).
-
-
2)
-
3. Danielsson, J., Andersson, A., Jarvet, J., Gräslund, A.: ‘15N relaxation study of the amyloid beta-peptide: structural propensities and persistence length’, Magn. Resonance Chem. (MRC), 2006, 44, pp. 114–121 (doi: 10.1002/mrc.1814).
-
-
3)
-
15. Wang, C.K., Liu, D.J., Wang, Z.X.: ‘Resonance light scattering as a powerful tool for sensitive detection of β-amyloid peptide by gold nanoparticle probes’, Chem. Commun., 2011, 47, pp. 9339–9341 (doi: 10.1039/c1cc12939b).
-
-
4)
- P.K. Jain , K.S. Lee , I.H. El-Sayed , M.A. El-Sayed . Calculated absorption and scattering properties of gold nanoparticle of different size, shape, and composition: applications in biological imaging and biomedicine. J. Phys. Chem. B , 14 , 7238 - 7248
-
5)
-
6. Sakono, M., Zako, T.: ‘Amyloid oligomers: formation and toxicity of Abeta oligomers’, FEBS J., 2010, 277, pp. 1348–1358 (doi: 10.1111/j.1742-4658.2010.07568.x).
-
-
6)
-
7. Yokoyama, K., Welchons, D.R.: ‘The conjugation of amyloid beta protein on the gold colloidal nanoparticles’ surfaces’, Nanotechnology, 2007, 18, pp. 105101–105107 (doi: 10.1088/0957-4484/18/10/105101).
-
-
7)
-
22. Zhou, L., Chan, K.H., Chu, L.W., et al: ‘Plasma amyloid-β oligomers level is a biomarker for Alzheimer's disease diagnosis’, Biochem. Biophys. Res. Commun., 2012, 423, pp. 697–702 (doi: 10.1016/j.bbrc.2012.06.017).
-
-
8)
-
13. Majzik, A., Fueloep, L., Csapo, E., et al: ‘Functionalization of gold nanoparticles with amino acid, beta-amyloid peptides and fragment’, Colloids Surf. B Biointerf., 2010, 81, pp. 235–241 (doi: 10.1016/j.colsurfb.2010.07.011).
-
-
9)
-
31. Geng, J., Li, M., Ren, J., Wang, E., Qu, X.G.: ‘Polyoxometalates as inhibitors of the aggregation of amyloid β peptides associated with Alzheimer's disease’’, Angew. Chem. Int. Ed., 2011, 50, pp. 4184–4188 (doi: 10.1002/anie.201007067).
-
-
10)
-
36. Outeiro, T.F.: ‘FlAsH illuminates Aβ aggregation’, Nat. Chem. Biol., 2011, 7, pp. 581–582 (doi: 10.1038/nchembio.636).
-
-
11)
-
39. Nilsson, M.R.: ‘Techniques to study amyloid fibril formation in vitro’, Methods, 2004, 34, pp. 151–160 (doi: 10.1016/j.ymeth.2004.03.012).
-
-
12)
-
33. Minkeviciene, R., Rheims, S., Dobszay, M.B., Zilberter, M.: ‘Amyloid beta-induced neuronal hyperexcitability triggers progressive epilepsy’, J. Neurosci., 2009, 29, pp. 3453–3462 (doi: 10.1523/JNEUROSCI.5215-08.2009).
-
-
13)
-
25. Millucci, L., Raggiaschi, R., Franceschini, D., Terstappen, G., Santucci, A.: ‘Rapid aggregation and assembly in aqueous solution of Aβ (25–35) peptide’, J. Biosci., 2009, 34, pp. 293–303 (doi: 10.1007/s12038-009-0033-3).
-
-
14)
-
28. Jayaraman, M., Kannayiram, G., Rajadas, J.: ‘Amyloid toxicity in skeletal myoblasts: implications for inclusion-body myositis’, Arch. Biochem. Biophys., 2008, 474, pp. 15–21 (doi: 10.1016/j.abb.2008.03.021).
-
-
15)
-
37. Kumar, S., Rezaei-Ghaleh, N., Terwel, D., et al: ‘Extracellular phosphorylation of the amyloid beta-peptide promotes formation of toxic aggregates during the pathogenesis of Alzheimer's disease’, EMBO J., 2011, 30, pp. 2255–2265 (doi: 10.1038/emboj.2011.138).
-
-
16)
-
9. Yokoyama, K., Gaulin, N.B., Cho, H., Briglio, N.M.: ‘Temperature dependence of conjugation of amyloid beta protein on the surfaces of gold colloidal nanoparticles’, J. Phys. Chem. A, 2010, 114, pp. 1521–1528 (doi: 10.1021/jp907880f).
-
-
17)
-
1. Kung, H.F.: ‘The β-amyloid hypothesis in Alzheimer's disease: seeing is believing’, ACS Med. Chem. Lett., 2012, 3, pp. 265–267 (doi: 10.1021/ml300058m).
-
-
18)
-
10. Liao, Y.H., Chang, Y.J., Yoshiike, Y., Chang, Y.C., Chen, Y.R.: ‘Negatively charged gold nanoparticles inhibit Alzheimer's amyloid-β fibrillization, induce fibril dissociation, and mitigate neurotoxicity’, Small, 2012, 8, pp. 3631–3639 (doi: 10.1002/smll.201201068).
-
-
19)
-
27. Clementi, M.E., Marini, S., Coletta, M., Orsini, F., Giardina, B., Misiti, F.: ‘Abeta(31–35) and Abeta(25–35) fragments of amyloid beta-protein induce cellular death through apoptotic signals: role of the redox state of methionine-35’, FEBS Lett., 2005, 579, pp. 2913–2918 (doi: 10.1016/j.febslet.2005.04.041).
-
-
20)
-
29. Yang, W., Sun, L.P., Weng, J., Chen, L., Zhang, Q.Q.: ‘Probing the interaction of bovine haemoglobin with gold nanoparticles’, IET Nanobiotechnol., 2012, 6, pp. 26–32 (doi: 10.1049/iet-nbt.2011.0029).
-
-
21)
-
14. Chan, H.M., Xiao, L., Yeung, K.M., et al: ‘Effect of surface-functionalized nanoparticles on the elongation phase of beta-amyloid (1–40) fibrillogenesis’, Biomaterials, 2012, 33, pp. 4443–4450 (doi: 10.1016/j.biomaterials.2012.03.024).
-
-
22)
-
26. Kubo, T., Nishimura, S., Kumagae, Y., Kaneko, Y.: ‘In vivo conversion of racemized beta-amyloid ((D-Ser 26) Aβ1–40) to truncated and toxic fragments ((D-Ser 26) Aβ25–35/40) and fragment presence in the brains of Alzheimer's patients’, J. Neurosci. Res., 2002, 70, pp. 474–483 (doi: 10.1002/jnr.10391).
-
-
23)
-
16. Wang, C.K., Liu, D.J., Wang, Z.X.: ‘Gold nanoparticle based dot-blot immunoassay for sensitively detecting Alzheimer's disease related β-amyloid peptide’, Chem. Commun., 2012, 48, pp. 8392–8394 (doi: 10.1039/c2cc33568a).
-
-
24)
-
2. Re, F., Airoldi, C., Zona, C., et al: ‘Beta amyloid aggregation inhibitors: small molecules as candidate drugs for therapy of Alzheimer's disease’, Curr. Med. Chem., 2010, 17, pp. 2990–3006 (doi: 10.2174/092986710791959729).
-
-
25)
-
11. Triulzi, R.C., Dai, Q., Zou, J., Leblanc, R.M., et al: ‘Photothermal ablation of amyloid aggregates by gold nanoparticles’, Colloids Surf. B Biointerf., 2008, 63, pp. 200–208 (doi: 10.1016/j.colsurfb.2007.12.006).
-
-
26)
-
32. Stine, W.B.Jr., Dahlgren, K.N., Krafft, G.A., LaDu, M.J.: ‘In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis’, J. Biol. Chem., 2003, 278, pp. 11612–11622 (doi: 10.1074/jbc.M210207200).
-
-
27)
-
20. Shoji, M.: ‘Biomarkers of the dementia’, Int. J. Alzheimer's Dis., 2011, 2011, pp. 564321.
-
-
28)
-
34. Xu, S.P., Yang, Y.Y., Xue, D., et al: ‘Cognitive-enhancing effects of polygalasaponin hydrolysate in Aβ25–35-induced amnesic mice’, Evid. Based Complement Alternat. Med., 2011, 2011, pp. 839720–839731.
-
-
29)
-
24. D'Ursi, A.M., Armenante, M.R., Guerrini, R., Salvadori, S., Sorrentino, G., Picone, D.: ‘Solution structure of amyloid beta-peptide (25–35) in different media’, J. Med. Chem., 2004, 47, pp. 4231–4238 (doi: 10.1021/jm040773o).
-
-
30)
-
21. Jack, C.R.Jr., Knopman, D.S., Jagust, W.J., et al: ‘Hypothetical model of dynamic biomarkers of the Alzheimer's pathological cascade’, Lancet Neurol., 2010, 9, pp. 119–128 (doi: 10.1016/S1474-4422(09)70299-6).
-
-
31)
-
17. Santos, A.N., Ewers, M., Minthon, L., et al: ‘Amyloid-β oligomers in cerebrospinal fluid are associated with cognitive decline in patients with Alzheimer's disease’, J. Alzheimer's Dis., 2012, 29, pp. 171–176..
-
-
32)
-
8. Yokoyama, K., Briglio, N.M., Hartati, D.S., Tsang, S.M.W., MacCormac, J.E., Welchons, D.R.: ‘Nanoscale size dependence in the conjugation of amyloid beta and ovalbumin proteins on the surface of gold colloidal particles’, Nanotechnology, 2008, 19, pp. 375101–375108 (doi: 10.1088/0957-4484/19/37/375101).
-
-
33)
-
18. Kingwell, K.: ‘Alzheimer disease: new insights into preclinical Alzheimer disease’, Nat. Rev. Neurol., 2013, 9, p. 4.
-
-
34)
-
38. Chen, C.E., Zhao, C.Q., Yang, X.J., Ren, J.S., Qu, X.G.: ‘Enzymatic manipulation of DNA-modified gold nanoparticles for screening G-quadruplex ligands and evaluating selectivities’, Adv. Mater., 2010, 22, pp. 389–393 (doi: 10.1002/adma.200901924).
-
-
35)
-
23. Dietrich, L.W., Funke, S.A., Kühbach, K., et al: ‘The amyloid-β oligomer count in cerebrospinal fluid is a biomarker for Alzheimer's disease’, J. Alzheimer's Dis., 2013, 34, pp. 985–994.
-
-
36)
-
19. Gao, C.M., Yam, A.Y., Wang, X., et al: ‘Aβ 40 oligomers identified as a potential biomarker for the diagnosis of Alzheimer's disease’, PLOS ONE, 2010, 5, p. e15725 (doi: 10.1371/journal.pone.0015725).
-
-
37)
-
4. Tomaselli, S., Esposito, V., Vangone, P., et al: ‘The alpha-to-beta conformational transition of Alzheimer's Abeta-(142) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of beta conformation seeding’, Chem. Biochem., 2006, 7, pp. 257–267.
-
-
38)
-
5. Ballatore, C., Lee, V.M., Trojanowski, J.Q.: ‘Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide’, Nat. Rev. Mol. Cell Biol., 2007, 8, pp. 101–112 (doi: 10.1038/nrm2101).
-
-
39)
-
12. Olmedo, I., Araya, E., Sanz, F., et al: ‘How changes in the sequence of the peptide CLPFFD-NH2 can modify the conjugation and stability of gold nanoparticles and their affinity for β-amyloid fibrils’, Bioconjugate Chem., 2008, 19, pp. 1154–1163 (doi: 10.1021/bc800016y).
-
-
1)