Commenced in January 2007
Frequency: Monthly
Edition: International
Paper Count: 30372
Comparative Studies on Interactions of Synthetic and Natural Compounds with Hen Egg-White Lysozyme

Authors: Seifollah Bahramikia

Abstract:

Amyloid aggregation of polypeptides is related to a growing number of pathologic states known as amyloid disorders. In recent years, blocking or reversing amyloid aggregation via the use of small compounds are considered as two useful approaches in hampering the development of these diseases. In this research, we have compared the ability of several manganese-salen derivatives, as synthetic compounds, and apigenin, as a natural flavonoid, to inhibit of hen egg-white lysozyme (HEWL) aggregation, as an in vitro model system. Different spectroscopic analyses such as Thioflavin T (ThT) and Anilinonaphthalene-8-sulfonic acid (ANS) fluorescence, Congo red (CR) absorbance along with transmission electron microscopy were used in this work to monitor the HEWL aggregation kinetic and inhibition. Our results demonstrated that both type of compounds were capable to prevent the formation of lysozyme amyloid aggregation in vitro. In addition, our data indicated that synthetic compounds had higher activity to inhibit of the β-sheet structures relative to natural compound. Regarding the higher antioxidant activities of the salen derivatives, it can be concluded that in addition to aromatic rings of each of the compounds, the potent antioxidant properties of salen derivatives contributes to lower lysozyme fibril accumulation.

Keywords: aggregation, apigenin, anti-amyloidogenic, hen egg white lysozyme, salen derivatives

Digital Object Identifier (DOI): doi.org/10.5281/zenodo.1094697

Procedia APA BibTeX Chicago EndNote Harvard JSON MLA RIS XML ISO 690 PDF Downloads 1740

References:


[1] C.M. Dobson, "Protein misfolding, evolution and disease”, Trends in biochemical sciences. vol. 24, pp. 329-332, 1999.
[2] E.H. Koo, P.T. Lansbury, J.W. Kelly, "Amyloid diseases: abnormal protein aggregation in neurodegeneration”, Proceedings of the National Academy of Sciences of the United States of America.vol. 96, pp. 9989- 9990, 1999.
[3] Z. Gazova, A. Bellova, Z. Daxnerova, J. Imrich, P. Kristian, J. Tomascikova, J. Bagelova, D. Fedunova, M. Antalik, "Acridine derivatives inhibit lysozyme aggregation”, European biophysics journal,. vol. 37, pp. 1261-1270, 2008.
[4] C.M. Dobson, "The structural basis of protein folding and its links with human disease”, Philosophical transactions of the Royal Society of London. Series B, Biological sciences,vol. 356, pp. 133-145, 2001.
[5] C.A. Ross, M.A. Poirier, "Protein aggregation and neurodegenerative disease”, Nature Medicine,Vol. 10, (Suppl) S10-S17, 2004.
[6] L.C. Serpell, M. Sunde, M.D. Benson, G.A. Tennent, M.B. Pepys, P.E. Fraser, "The protofilament substructure of amyloid fibrils”, Journal of Molecular Biology, Vol. 300, pp.1033-1039,2000.
[7] M.N.N. Vieira, J.D. Figueroa-Villar, M.N.L. Meirelles, S.T. Ferreira, F.G. De Felice, "Small Molecule Inhibitors of Lysozyme Amyloid Aggregation”, Cell Biochemistry and Biophysics,Vol. 44, pp. 549-553, 2006.
[8] L.N. Arnaudov, R. de Vries, Thermally induced fibrillar aggregation of Hen Egg White Lysozyme, Biophysical Journal, vol. 88, pp. 515-526, 2005.
[9] Y. Porat, A. Abramowitz, E. Gazit, "Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism”, Chemical Biology & Drug Design, Vol. 67,pp. 27-37, 2006.
[10] M. Baudry, S. Etienne, A. Bruce, M. Palucki, E. Jacobsen, B. Malfroy, "Salen–manganese complexes are superoxide dismutase mimics”, Biochemical and biophysical research communications,Vol. 192, pp. 964-968, 1993.
[11] M.R. Nilsson, "Techniques to study amyloid fibril formation in vitro”, Methods, vol. 34, no. 1, pp. 151-160, 2004.
[12] A. Rabiee, A. Ebrahim-Habibi, L. Navidpour, D. Morshedi, A. Ghasemi, M. Sabbaghian, M. Nemati-Lay, M. Nemat-Gorgani, "Benzofuranone Derivatives as Effective Small Molecules Related to Insulin Amyloid Fibrillation: A Structure-Function Study”, Chemical Biology & Drug Design, vol. 78, pp. 659-666, 2011.
[13] J.H. Byun, H. Kim, Y. Kim, I. Mook-Jung, D.J. Kim, W.K. Lee, K.H. Yoo, "Aminostyrylbenzofuran derivatives as potent inhibitors for Abeta fibril formation”, Bioorganic and Medicinal Chemistry Letter,Vol. 18,pp. 5591-5593, 2008.