The role of metal ions in the fibrillization of lysozyme and insulin in vitro
Keywords:
amyloid fibrils, insulin, lysozyme, metal ions, Thioflavin T
Abstract
The effects of metal ions on the fibrillization of lysozyme and insulin were investigated using a
Thioflavin T fluorescence assay and transmission electron microscopy. The incubation of the proteins in
acidic buffer at high temperature in the presence of substoichiometric concentrations of Сu2+, Zn2+, Fe3+
and Al3+ primarily led to the decrease in lag phase of fibril growth and protein aggregation rate compared to those in control samples. Furthermore, Сu2+ and Fe3+ showed a stronger influence on the protein fibrillization than Zn2+ and Al3+. Specifically, Сu2+ and Fe3+ provoked the formation of insulin amyloid fibrils, having a «fuzzy» appearance, while the amyloid-like insulin aggregates grew in the presence of Zn2+. These results highlight the potential of metal ions as prospective therapeutic agents against human«conformational» diseases.
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References
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3. Role of metal dyshomeostasis in Alzheimer disease / D. J. Bonda, H. Lee, J. Blair [et. al.] // Metallomics. – 2011. – Vol. 3. – P. 267–270.
4. Iron and aluminum increase in the substantia nigra of patients with Parkinson's disease: an X-ray microanalysis / E. C. Hirsch, J. P. Brandel, P. Galle [et. al.] // J. Neurochem. – 1991. – Vol. 56. – P. 446–451.
5. Copper (II) inhibits in vitro conversion of prion protein into amyloid fibrils / O. V. Bocharova, L. Breydo, V. V. Salnikov [et.al.] // Biochemistry. – 2005. – Vol. 44. – P. 6776–6687.
6. Alies B. The role of metal ions in amyloid formation: general principles from model peptides / B. Alies, C. Hureau, P. Faller // Metallomics. – 2013. – Vol. 5. – P. 183–192.
7. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism / L. Nielsen, R. Khurana, A. Coats [et. al.] // Biochemistry. – 2001. – Vol. 40. – P. 6036–6046.
8. Metals and amyloid-beta in Alzheimer's disease / C. J. Maynard, A. I. Bush, C. L. Masters [et. al.] // Int. J. Exp. Pathol. – 2005. – Vol. 86. – P. 147–159.
9. Aluminum, copper, iron and zinc differentially alter amyloid-Aβ1-42 aggregation and toxicity / S. Bolognin, L. Messori, D. Drago [et. al.] // Int. J. Biochem. Cell Biol. – 2011. – Vol. 43. – P. 877–885.
10. Effect of Fe3O4 magnetic nanoparticles on lysozyme amyloid aggregation / A. Bellova, E. Bystrenova, M. Koneracka [et. al.] // Nanotechnology. – 2010. – Vol. 21. – P. 065103.
11. Metals accelerate the formation and direct the structure of amyloid fibrils of NAC / A. Khan, A. E. Ashcroft, V. Higenell [et. al.] // J. Inorg. Biochem. – 2005. – Vol. 99. – P. 1920–1927.
12. Copper is a potent inhibitor of the propensity for human ProIAPP1-48 to form amyloid fibrils in vitro / C. Exley, M. Mold, E. Shardlow [et. al.] // J. Diabet. Res. Clin. Med. – 2012. – Vol. 1. – P. 1–6.
13. Recent development of bifunctional small molecules to study metal-amyloid-β species in Alzheimer's disease / J. J. Braymer, A. S. Detoma, J. S. Choi [et. al.] // Int. J. Alzheimer’s Dis. – 2011. – Vol. 623051. – P. 1–9.
14. Hydrogen peroxide can be generated by tau in the presence of Cu (II) / X. Y. Su, W. H. Wu, Z. P. Huang [et. al.] // Biochem. Biophys. Res. Commun. – 2007. – Vol. 358. – P. 661–665.
15. Morante S. The role of metals in beta-amyloid peptide aggregation: X-Ray spectroscopy and numerical simulations / S. Morante // Curr. Alzheimer. Res. – 2008. – Vol. 5. – P. 508–524.
16. Tõugu V. Interactions of Zn (II) and Cu (II) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity / V. Tõugu, A. Tiiman, P. Palumaa // Metallomics. – 2011. – Vol. 3. – P.250–261.
17. Faller P. Role of metal ions in the f-assembly of the Alzheimer’s amyloid-β peptide / P. Faller, C. Hureau, O. Berthoumieu // Inorg. Chem. – 2013. – Vol. 52. – P. 12193–12206.
18. Does aluminium bind to histidine? An NMR investigation of amyloid β12 and amyloid β16 fragments / P. Narayan, B. Krishnarjuna, V. Vishwanathan [et. al.] // Chem. Biol. Drug Des. – 2013. – Vol. 82. – P. 48–59.
19. Uversky V. N. Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure / V. N. Uversky, J. Li, A. L. Fink // J. Biol. Chem. – 2001. – Vol. 276. – P. 44284–44296.
Cited
How to Cite
Vus, K. O., Trusova, V. M., Gorbenko, G. P., Slobozhanina, E. I., Lukyanenko, L. M., Sood, R., & Kinnunen, P. (1). The role of metal ions in the fibrillization of lysozyme and insulin in vitro. Biophysical Bulletin, 2(30). Retrieved from https://periodicals.karazin.ua/biophysvisnyk/article/view/1596
Section
Molecular biophysics
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