The Size Effect of Fe Nanoparticles on Hen Egg-White Lyzozyme Structure and Activity

Document Type : Research Article

Authors

1 Biochemistry and Biophysics Research Center, University of Tehran, Tehran, I.R. IRAN

2 Faculty of Chemistry, Razi University Kermanshah, Kermanshah, I.R. IRAN

3 Pharmaceutical Sciences Research Center, Health Research Institute, Kermanshah University of Medical Sciences, Kermanshah, I.R. IRAN

Abstract

Superparamagnetic iron oxide nanoparticles (SPIONs) with Fe3O4 molecular composition were considered for the study of protein interactions and drug delivery. Considering that SPIONs play a significant role in nanomedicine and drug delivery systems, investigating the interaction between SPIONs and a model protein and its structural and functional changes can be enlightening in scientific research. SPIONs with sizes of 20, 50, and 100 nm were selected. The UV-visible spectroscopic study showed the interaction between protein-nanoparticles. Rotational exponential imaging was used to measure the changes in the secondary structure of lysozyme in interaction with SPIONs. A significant reduction in the helical structures of the protein was observed. Protein fluorescence quenching analysis was used to understand the nature of protein-nanoparticle interaction. The interaction of SPIONs and lysozyme showed a combination of dynamic and static quenching. The activity and enzymatic properties of lysozyme attached to SPIONs were measured compared to free lysozyme. The activity decreased dramatically in all sizes of SPIONs, but the Km changed under different reaction conditions.

Keywords

Main Subjects

References

[1] Larsericsdotter H., Oscarsson S., Buijs J., Thermodynamic Analysis of Proteins Adsorbed on Silica Particles: Electrostatic Effects, Journal of colloid and interface science, 237(1): 98-103 (2001).
[2] Billsten P., Carlsson U., Jonsson B.H., Olofsson G., Höök F., Elwing H., Conformation of Human Carbonic Anhydrase II Variants Adsorbed to Silica Nanoparticles, Langmuir, 15(19): 6395-6399 (1999).
[3] Hobara D., Imabayashi S.i., Kakiuchi T., Preferential Adsorption of Horse Heart Cytochrome c on Nanometer-Scale Domains of a Phase-Separated Binary Self-Assembled Monolayer of 3-Mercaptopropionic Acid and 1-Hexadecanethiol on Au (111), Nano Letters, 2(9): 1021-1025 (2002).
[4] Roach P., Farrar D., Perry C.C., Interpretation of Protein Adsorption: Surface-Induced Conformational Changes, Journal of the American Chemical Society, 127(22): 8168-8173 (2005).
[5] Janin J., Bahadur R.P., Chakrabarti P., Protein–Protein Interaction and Quaternary Structure, Quarterly reviews of biophysics, 41(2): 133-180 (2008).
[6] Degterev A., Lugovskoy A., Cardone M., Mulley B., Wagner G., Mitchison T., Yuan J., Identification of Small-Molecule Inhibitors of Interaction Between the BH3 Domain and Bcl-xL, Nature cell biology, 3(2): 173-182 (2001).
[7] Shang W., Nuffer J.H., Muñiz‐Papandrea V.A., Colón W., Siegel R.W., Dordick J.S., Cytochrome c on Silica Nanoparticles: Influence of Nanoparticle Size on Protein Structure, Stability, and Activity, Small, 5(4): 470-476 (2009).
[8] Kashanian F., Habibi-Rezaei M., Bagherpour A.R., Seyedarabi A., Moosavi-Movahedi A.A., Magnetic Nanoparticles as Double-Edged Swords: Concentration-Dependent Ordering or Disordering Effects on Lysozyme, RSC advances, 7(86): 54813-54822 (2017).
[9] Akhtar Kh., Shah A., Zubair N., Javed K., Chemical Dynamics of Monodispersed Iron Oxide Nanoparticles. Iranian Journal of Chemistry and Chemical Engineering (IJCCE), 38(5): 21-30 (2019).
[10] Fleming A., On a Remarkable Bacteriolytic Element Found in Tissues and Secretions, Proceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character, 93(653): 306-317 (1922).
[11] Sagermann M., Matthews B.W., Crystal Structures of A T4-Lysozyme Duplication-Extension Mutant Demonstrate that the Highly Conserved Β-Sheet Region has Low Intrinsic Folding Propensity, Journal of molecular biology, 316(4): 931-940 (2002).
[12] Tagashira A., Nishi K., Sugahara T., Lysozyme from hen Egg White Ameliorates Lipopolysaccharide-Induced Systemic Inflammation in Mice, Cytotechnology, 71(2): 497-506 (2019).
[13] Takahashi M., Okakura Y., Takahashi H., Imamura M., Takeuchi A., Shidara H., Kuda T., Kimura B., Heat-Denatured Lysozyme Could be A Novel Disinfectant for Reducing Hepatitis A Virus and Murine Norovirus on Berry Fruit, Int J Food Microbiol, 266: 104-108 (2018).
[14] Kuehner D.E., Engmann J., Fergg F., Wernick M., Blanch H.W., Prausnitz J.M., Lysozyme Net Charge and Ion Binding in Concentrated Aqueous Electrolyte Solutions, The Journal of Physical Chemistry B, 103(8): 1368-1374 (1999).
[15] Swaminathan R., Ravi V.K., Kumar S., Kumar M.V., Chandra N., Lysozyme: A Model Protein for Amyloid Research, Advances in protein chemistry and structural biology, 84: 63-111 (2011).
[16] Mohamadpour M., Pirdashti M., Shahrokhi B., Rostami A.A., Response Surface Methodology for the Evaluation of Lysozyme Partitioning in Poly (Vinyl Pyrrolidone) and Potassium Phosphate Aqueous Two-Phase System. Iranian Journal of Chemistry and Chemical Engineering (IJCCE), 38(5): 197-208 (2019).
[17] Lesnierowski G., Kijowski J., Lysozyme, Bioactive egg compounds, 33-42 (2007).
[18] Ghosh A., Brinda K., Vishveshwara S., Dynamics of Lysozyme Structure Network: Probing the Process of Unfolding, Biophysical journal, 92(7): 2523-2535 (2007).
[19] Knubovets T., Osterhout J.J., Connolly P.J., Klibanov A.M., Structure, Thermostability, and Conformational Flexibility of Hen Egg-White Lysozyme Dissolved in Glycerol, Proceedings of the National Academy of Sciences, 96(4): 1262-1267 (1999).
[20] Pepys M.B., Hawkins P.N., Booth D.R., Vigushin D.M., Tennent G.A., Soutar A.K., Totty N., Nguyen O., Blake C.C., Terry C.J., Feest T.G., Human Lysozyme Gene Mutations cause Hereditary Systemic Amyloidosis, Nature, 362(6420): 553-557 (1993).
[21] Cai H., Yao P., In Situ Preparation of Gold Nanoparticle-Loaded Lysozyme-Dextran Nanogels and Applications for Cell Imaging and Drug Delivery, Nanoscale, 5(7): 2892-2900 (2013).
[22] Kwok P.C., Tunsirikongkon A., Glover W., Chan H.K., Formation of Protein Nano-Matrix Particles with Controlled Surface Architecture for Respiratory Drug Delivery, Pharm Res, 28(4): 788-796 (2011).
[23] Peng Z.G., Hidajat K., Uddin M.S., Adsorption and Desorption of Lysozyme on Nano-Sized Magnetic Particles and its Conformational Changes, Colloids Surf B Biointerfaces, 35(3-4): 169-174 (2004).
[24] Shang W., Nuffer J.H., Dordick J.S., Siegel R.W., Unfolding of Ribonuclease A on Silica Nanoparticle Surfaces, Nano letters, 7(7): 1991-1995 (2007).
[25] Vertegel A.A., Siegel R.W., Dordick J.S., Silica Nanoparticle Size Influences the Structure and Enzymatic Activity of Adsorbed Lysozyme, Langmuir, 20(16): 6800-6807 (2004).
[26] Eslami Moghadam M., Mansouri-Torshizi H., Saidifar M., Investigation of the Interaction of Antitumor Palladium and Platinum Complexes of Ethyldithiocarbamate with Human Serum Albumin. Nashrieh Shimi va Mohandesi Shimi Iran, 37(4): 155-166 (2019).
[27] Chakraborti S., Chatterjee T., Joshi P., Poddar A., Bhattacharyya B., Singh S.P., Gupta V., Chakrabarti P., Structure and Activity of Lysozyme on Binding to ZnO Nanoparticles, Langmuir, 26(5): 3506-3513 (2009).
[28] Mahmoudi M., Shokrgozar M.A., Sardari S., Moghadam M.K., Vali H., Laurent S., Stroeve P., Irreversible Changes in Protein Conformation due to Interaction with Superparamagnetic Iron Oxide Nanoparticles, Nanoscale, 3(3): 1127-1138 (2011).
]29[ Perkampus H.H., "UV-VIS Spectroscopy and its Applications". Springer Science & Business Media (2013).
]30[ Worthington C.C., "Worthington Enzyme Manual: Enzymes and Related Biochemicals". Worthington Biochemical Corporation (1988).
[31] Stern O., Volmer M., Über Die Abklingzeit der Fluoreszenz, phys. Z, 20: 183-188 (1919).
[32] Lakowicz J.R., "Principles of Fluorescence Spectroscopy". Springer (2006).
[33] Lehrer S., Solute Perturbation of Protein Fluorescence. Quenching of the Tryptophyl Fluorescence of Model Compounds and of Lysozyme by Iodide Ion, Biochemistry, 10(17): 3254-3263 (1971).
[34] Karukstis K.K., Gruber S.M., Fruetel J.A., Boegeman S.C., Quenching of Chlorophyll Fluorescence by Substituted Anthraquinones, Biochimica et Biophysica Acta (BBA)-Bioenergetics, 932: 84-90 (1988).
[35] Karukstis K.K., Boegeman S.C., Fruetel J.A., Gruber S.M., Terris M.H., Multivariate Analysis of Photosystem II Fluorescence Quenching by Substituted Benzoquinones and Naphthoquinones, Biochimica et Biophysica Acta (BBA)-Bioenergetics, 891(3): 256-264 (1987).
[36] Rohatgi-Mukherjee K., "Fundamentals of Photochemistry". New Age International (1978).
[37] Le Chatelier H., Estimation of Firedamp by Flammability Limits, Annals of Mines, 19(8): 388-395 (1891).
[38] Ding F., Zhao G., Huang J., Sun Y., Zhang L., Fluorescence Spectroscopic Investigation of the Interaction between Chloramphenicol and Lysozyme, European journal of medicinal chemistry, 44(10): 4083-4089 (2009).
[39] Liu X.F., Xia Y.M., Fang Y., Effect of Metal Ions on the Interaction between Bovine Serum Albumin and Berberine Chloride Extracted from a Traditional Chinese Herb Coptis Chinensis Franch, Journal of inorganic biochemistry, 99(7): 1449-1457 (2005).
[40] Ji Z., Yuan H., Liu M., Hu J., 1H-NMR Study of the Effect of Acetonitrile on the Interaction of Ibuprofen with Human Serum Albumin. Journal of pharmaceutical and biomedical analysis, 30(1): 151-159 (2002).
[41] Jelesarov I., Bosshard H.R., Isothermal Titration Calorimetry and Differential Scanning Calorimetry as Complementary Tools to Investigate the Energetics of Biomolecular Recognition. Journal of molecular recognition, 12(1): 3-18 (1999).
Nashrieh Shimi va Mohandesi Shimi Iran
Volume 42, Issue 3 - Serial Number 109
September 2024
Pages 169-187

Files

Share

How to cite

Statistics