513
Views
32
CrossRef citations to date
0
Altmetric
Articles

Effects of hesperidin, a flavanone glycoside interaction on the conformation, stability, and aggregation of lysozyme: multispectroscopic and molecular dynamic simulation studies?

, , , , &
Pages 1866-1879 | Received 29 Aug 2014, Accepted 08 Oct 2014, Published online: 05 Nov 2014

References

  • Ahmad, B., & Lapidus, L. J. (2012). Curcumin prevents aggregation in α-synuclein by increasing reconfiguration rate. Journal of Biological Chemistry, 287, 9193–9199.10.1074/jbc.M111.325548
  • Ahmad, E., Rabbani, G., Zaidi, N., Khan, M. A., Qadeer, A., Ishtikhar, M., … Khan, R. H. (2013). Revisiting ligand-induced conformational changes in proteins: Essence, advancements, implications and future challenges. Journal of Biomolecular Structure & Dynamics, 31, 630–648.
  • Al-Ashaal, H. A., & El-Sheltawy, S. T. (2011). Antioxidant capacity of hesperidin from citrus peel using electron spin resonance and cytotoxic activity against human carcinoma cell lines. Pharmaceutical Biology, 49, 276–282.10.3109/13880209.2010.509734
  • Borana, M. S., Mishra, P., Pissurlenkar, R. R., Hosur, R. V., & Ahmad, B. (2014). Curcumin and kaempferol prevent lysozyme fibril formation by modulating aggregation kinetic parameters. Biochimica et Biophysica Acta (BBA) – Proteins and Proteomics, 1844, 670–680.10.1016/j.bbapap.2014.01.009
  • Bourassa, P., Bariyanga, J., & Tajmir-Riahi, H. A. (2013). Binding sites of resveratrol, genistein, and curcumin with milk α- and β-caseins. The Journal of Physical Chemistry B, 117, 1287–1295.10.1021/jp3114557
  • Bowers, K. J., Chow, E., Xu, H., Dror, R. O., Eastwood, M. P., Gregersen, B. A., … Shaw, D. E. (2006, 11–17). Scalable algorithms for molecular dynamics simulations on commodity clusters. Proceedings of the ACM/IEEE Conference on Supercomputing (SC06), Tampa, FL.
  • Calhoun, D. B., Vanderkooi, J. M., Holtom, G. R., & Englander, S. W. (1986). Protein fluorescence quenching by small molecules: Protein penetration versus solvent exposure. Proteins: Structure, Function, and Genetics, 1, 109–115.10.1002/(ISSN)1097-0134
  • Celej, M. S., Montich, G. G., & Fidelio, G. D. (2003). Protein stability induced by ligand binding correlates with changes in protein flexibility. Protein Science, 12, 1496–1506.10.1110/(ISSN)1469-896X
  • Chiti, F., & Dobson, C. M. (2006). Protein misfolding, functional amyloid, and human disease. Annual Review of Biochemistry, 75, 333–366.10.1146/annurev.biochem.75.101304.123901
  • Daniels, K. G., Tonthat, N. K., McClure, D. R., Chang, Y. C., Liu, X., Schumacher, M. A., … Fierke, Carol A. (2014). Ligand concentration regulates the pathways of coupled protein folding and binding. Journal of the American Chemical Society, 136, 822–825.10.1021/ja4086726
  • de Azevedo, W. F. Jr., & Dias, R. (2008). Experimental approaches to evaluate the thermodynamics of protein–drug interactions. Current Drug Targets, 9, 1071–1076.10.2174/138945008786949441
  • Ding, F., Diao, J. X., Sun, Y., & Sun, Y. (2012a). Bioevaluation of human serum albumin–hesperidin bioconjugate: Insight into protein vector function and conformation. Journal of Agricultural and Food Chemistry, 60, 7218–7228.10.1021/jf300424w
  • Ding, F., Sun, Y., Diao, J. X., Li, X. N., Yang, X. L., Sun, Y., & Zhang, L. (2012). Features of the complex of food additive hesperidin to hemoglobin. Journal of Photochemistry and Photobiology B: Biology, 106, 53–60.10.1016/j.jphotobiol.2011.10.004
  • Eftink, M. R. (1991). Fluorescence techniques for studying protein structure. Methods of Biochemical Analysis, 35, 127–205.10.1002/SERIES2180
  • Eftink, M. R., & Ghiron, C. A. (1981). Fluorescence quenching studies with proteins. Analytical Biochemistry, 114, 199–227.10.1016/0003-2697(81)90474-7
  • Emim, J. A., Oliveira, A. B., & Lapa, A. J. (1994). Pharmacological evaluation of the anti-inflammatory activity of a citrus bioflavonoid, hesperidin, and the isoflavonoids, duartin and claussequinone, in rats and mice. Journal of Pharmacy and Pharmacology, 46, 118–122.10.1111/jphp.1994.46.issue-2
  • Frare, E., De Laureto, P. P., Zurdo, J., Dobson, C. M., & Fontana, A. (2004). A highly amyloidogenic region of hen lysozyme. Journal of Molecular Biology, 340, 1153–1165.10.1016/j.jmb.2004.05.056
  • Frare, E., Mossuto, M. F., de Laureto, P. P., Dumoulin, M., & Dobson, C. M. (2006). Identification of the core structure of lysozyme amyloid fibrils by proteolysis. Journal of Molecular Biology, 361, 551–561.10.1016/j.jmb.2006.06.055
  • Freitas, P. G., Barbosa, A. F., Saraiva, L. A., Camps, I., da Silveira, N. J. F., Veloso, M. P., … Schneedorf, J. M. (2012). Mangiferin binding to serum albumin is non-saturable and induces conformational changes at high concentrations. Journal of Luminescence, 132, 3027–3034.10.1016/j.jlumin.2012.06.020
  • Friesner, R. A., Banks, J. L., Murphy, R. B., Halgren, T. A., Klicic, J. J., Mainz, D. T., … Shenkin, P. S. (2004). Glide: A new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. Journal of Medicinal Chemistry, 47, 1739–1749.10.1021/jm0306430
  • Friesner, R. A., Murphy, R. B., Repasky, M. P., Frye, L. L., Greenwood, J. R., Halgren, T. A., … Mainz, D. T. (2006). Extra precision glide: Docking and scoring incorporating a model of hydrophobic enclosure for protein−ligand complexes. Journal of Medicinal Chemistry, 49, 6177–6196.10.1021/jm051256o
  • Ghosh, K. S., Sahoo, B. K., & Dasgupta, S. (2008). Spectrophotometric studies on the interaction between (−)-epigallocatechin gallate and lysozyme. Chemical Physics Letters, 452, 193–197.10.1016/j.cplett.2007.12.018
  • Goldberg, M. E., Rudolph, R., & Jaenicke, R. (1991). A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry, 30, 2790–2797.10.1021/bi00225a008
  • Guo, Z., Mohanty, U., Noehre, J., Sawyer, T. K., Sherman, W., & Krilov, G. (2010). Probing the α-helical structural stability of stapled p53 peptides: Molecular dynamics simulations and analysis. Chemical Biology & Drug Design, 75, 348–359.
  • Halgren, T. A., Murphy, R. B., Friesner, R. A., Beard, H. S., Frye, L. L., Pollard, W. T., & Banks, J. L. (2004). Glide: A new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. Journal of Medicinal Chemistry, 47, 1750–1759.10.1021/jm030644s
  • Iranfar, H., Rajabi, O., Salari, R., & Chamani, J. (2012). Probing the interaction of human serum albumin with ciprofloxacin in the presence of silver nanoparticles of three sizes: multispectroscopic and ζ potential investigation. The Journal of Physical Chemistry B, 116, 1951–1964.10.1021/jp210685q
  • Kamtekar, N., Pandey, A., Agrawal, N., Pissurlenkar, R. R., Borana, M., & Ahmad, B. (2013). Interaction of multimicrobial synthetic inhibitor 1,2-bis(2-benzimidazolyl)-1,2-ethanediol with serum albumin: Spectroscopic and computational studies. PLoS ONE, 8, e53499.10.1371/journal.pone.0053499
  • Kelly, S. M., & Price, N. C. (1997). The application of circular dichroism to studies of protein folding and unfolding. Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology, 1338, 161–185.10.1016/S0167-4838(96)00190-2
  • Knowles, T. P., Fitzpatrick, A. W., Meehan, S., Mott, H. R., Vendruscolo, M., Dobson, C. M., & Welland, M. E. (2007). Role of intermolecular forces in defining material properties of protein nanofibrils. Science, 318, 1900–1903.10.1126/science.1150057
  • Knubovets, T., Osterhout, J. J., Connolly, P. J., & Klibanov, A. M. (1999). Structure, thermostability, and conformational flexibility of hen egg-white lysozyme dissolved in glycerol. Proceedings of the National Academy of Sciences, 96, 1262–1267.10.1073/pnas.96.4.1262
  • Kumar, S., & Swaminathan, R. (2007). Employing the fluorescence anisotropy and quenching kinetics of tryptophan to hunt for residual structures in denatured proteins. Journal of Chemical Sciences, 119, 141–145.10.1007/s12039-007-0021-9
  • Kundu, T., Chowdhury, A. D., De, D., Mobin, S. M., Puranik, V. G., Datta, A., & Lahiri, G. K. (2012). Selective recognition of fluoride and acetate by a newly designed ruthenium framework: Experimental and theoretical investigations. Dalton Transactions, 41, 4484–4496.10.1039/c2dt12126c
  • Lakowicz, J. R. (2006). Principles of fluorescence spectroscopy (3rd ed.). New York, NY: Springer.10.1007/978-0-387-46312-4
  • Miller, J. N. (1979). Recent advances in molecular luminescence analysis. Proceedings of the Analytical Division of the Chemical Society, 16, 203–208.
  • Mitra, P., Banerjee, M., Biswas, S., & Basu, S. (2013). Protein interactions of merocyanine 540: Spectroscopic and crystallographic studies with lysozyme as a model protein. Journal of Photochemistry and Photobiology B: Biology, 121, 46–56.10.1016/j.jphotobiol.2013.02.010
  • Morrow, J. A., Segall, M. L., Lund-Katz, S., Phillips, M. C., Knapp, M., Rupp, B., & Weisgraber, K. H. (2000). Differences in stability among the human apolipoprotein E isoforms determined by the amino-terminal domain. Biochemistry, 39, 11657–11666.10.1021/bi000099m
  • Necula, M., Kayed, R., Milton, S., & Glabe, C. G. (2007). Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct. Journal of Biological Chemistry, 282, 10311–10324.10.1074/jbc.M608207200
  • Olsson, T. S. G., Williams, M. A., Pitt, W. R., & Ladbury, J. E. (2008). The thermodynamics of protein–ligand interaction and solvation: Insights for ligand design. Journal of Molecular Biology, 384, 1002–1017.10.1016/j.jmb.2008.09.073
  • Pasban Ziyarat, F., Asoodeh, A., Sharif Barfeh, Z., Pirouzi, M., & Chamani, J. (2014). Probing the interaction of lysozyme with ciprofloxacin in the presence of different-sized Ag nano particles by multispectroscopic techniques and isothermal titration calorimetry. Journal of Biomolecular Structure & Dynamics, 32, 613–629.
  • Porat, Y., Abramowitz, A., & Gazit, E. (2006). Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism. Chemical Biology & Drug Design, 67, 27–37.
  • Ross, P. D., & Rekharsky, M. V. (1996). Thermodynamics of hydrogen bond and hydrophobic interactions in cyclodextrin complexes. Biophysical Journal, 71, 2144–2154.10.1016/S0006-3495(96)79415-8
  • Ross, P. D., & Subramanian, S. (1981). Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20, 3096–3102.10.1021/bi00514a017
  • Sarzehi, S., & Chamani, J. (2010). Investigation on the interaction between tamoxifen and human holo-transferrin: Determination of the binding mechanism by fluorescence quenching, resonance light scattering and circular dichroism methods. International Journal of Biological Macromolecules, 47, 558–569.10.1016/j.ijbiomac.2010.08.002
  • Schön, A., Brown, R. K., Hutchins, B. M., & Freire, E. (2013). Ligand binding analysis and screening by chemical denaturation shift. Analytical Biochemistry, 443, 52–57.10.1016/j.ab.2013.08.015
  • Schrödinger release 2014-1: Maestro, version 9.7; Glide, version 6.2; Prime, version 3.5; Desmond molecular dynamics system, version 3.7. (2014). New York, NY: Schrödinger, LLC.
  • Shivakumar, D., Williams, J., Wu, Y., Damm, W., Shelley, J., & Sherman, W. (2010). Prediction of absolute solvation free energies using molecular dynamics free energy perturbation and the OPLS force field. Journal of Chemical Theory and Computation, 6, 1509–1519.10.1021/ct900587b
  • Torres-Bugeau, C. M., Avila, C. L., Raisman-Vozari, R., Papy-Garcia, D., Itri, R., Barbosa, L. R., … Chehín, R. N. (2012). Characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase early amyloid-like oligomers and their implication in α-synuclein aggregation. Journal of Biological Chemistry, 287, 2398–2409.10.1074/jbc.M111.303503
  • Venyaminov, S., Yu, J. T., & Yang, J. T. (1996). Circular dichroism and the conformational analysis of biomolecules, (G. D. Fasman, ed., pp. 69–104). New York, NY: Plenum.
  • Wallevik, K. (1973). Reversible denaturation of human serum albumin by pH, temperature and guanidine hydrochloride. Journal of Biological Chemistry, 245, 2650–2655.
  • Wang, S. S., Liu, K. N., & Lee, W. H. (2009). Effect of curcumin on the amyloid fibrillogenesis of hen egg-white lysozyme. Biophysical Chemistry, 144, 78–87.10.1016/j.bpc.2009.06.010
  • Ware, W. R. (1962). Oxygen quenching of fluorescence in solution: An experimental study of the diffusion process. The Journal of Physical Chemistry, 66, 455–458.10.1021/j100809a020
  • West, G. M., Tucker, C. L., Xu, T., Park, S. K., Han, X., Yates, J. R., 3rd, & Fitzgerald, M. C. (2010). Quantitative proteomics approach for identifying protein-drug interactions in complex mixtures using protein stability measurements. Proceedings of the National Academy of Sciences, 107, 9078–9082.10.1073/pnas.1000148107
  • Youdim, K. A., Dobbie, M. S., Kuhnle, G., Proteggente, A. R., Abbott, N. J., & Rice-Evans, C. (2003). Interaction between flavonoids and the blood–brain barrier: In vitro studies. Journal of Neurochemistry, 85, 180–192.10.1046/j.1471-4159.2003.01652.x
  • Zolfagharzadeh, M., Pirouzi, M., Asoodeh, A., Saberi, M. R., & Chamani, J. (2014). A comparison investigation of DNP-binding effects to HSA and HTF by spectroscopic and molecular modeling techniques. Journal of Biomolecular Structure & Dynamics, 32, 1936–1952.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.