title: Investigating the Interaction of Fe Nanoparticles with Lysozyme by Biophysical and Molecular Docking Studies.
abstract: Herein, the interaction of hen egg white lysozyme (HEWL) with iron nanoparticle (Fe NP) was investigated by spectroscopic and docking studies. The zeta potential analysis revealed that addition of Fe NP (6.45±1.03 mV) to HEWL (8.57±0.54 mV) can cause to greater charge distribution of nanoparticle-protein system (17.33±1.84 mV). In addition, dynamic light scattering (DLS) study revealed that addition of Fe NP (92.95±6.11 nm) to HEWL (2.68±0.37 nm) increases suspension potential of protein/nanoparticle system (51.17±3.19 nm). Fluorescence quenching studies reveled that both static and dynamic quenching mechanism occur and hydrogen bond and van der Waals interaction give rise to protein-NP system. Synchronous fluorescence spectroscopy of HEWL in the presence of Fe NP showed that the emission maximum wavelength of tryptophan (Trp) residues undergoes a red-shift. ANS fluorescence data indicated a dramatic exposure of hydrophobic residues to the solvent. The considerable reduction in melting temperature (T(m)) of HEWL after addition of Fe NP determines an unfavorable interaction system. Furthermore circular dichoroism (CD) experiments demonstrated that, the secondary structure of HEWL has not changed with increasing Fe NP concentrations; however, some conformational changes occur in tertiary structure of HEWL. Moreover, protein-ligand docking study confirmed that the Fe NP forms hydrogen bond contacts with HEWL.
authors: Department of Biology, Islamic Azad University, Science and Research Branch, Tehran, Iran.
authors: Zahra
authors: Z
authors: Aghili
authors: Department of Biology, Islamshahr Branch, Islamic Azad University, Islamshahr, Iran.
authors: Saba
authors: S
authors: Taheri
authors: MEMS & NEMS Lab, Department of Electrical and Computer Engineering, University of Tehran, Tehran, Iran.
authors: Hojjat Alizadeh
authors: HA
authors: Zeinabad
authors: Young Researchers and Elite Club, Islamshahr Branch, Islamic Azad University, Islamshahr, Iran.
authors: Leila
authors: L
authors: Pishkar
authors: Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran.|Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran.
authors: Ali Akbar
authors: AA
authors: Saboury
authors: Department of Biology, Islamic Azad University, Science and Research Branch, Tehran, Iran.
authors: Arash
authors: A
authors: Rahimi
authors: Department of Nanotechnology, Faculty of Advance Science and Technology, Islamic Azad University of Pharmaceutical Sciences (IAUPS), Tehran, Iran.
authors: Mojtaba
authors: M
authors: Falahati
mesh_terms: D000818:Animals; D002942:Circular Dichroism; D000067493:Dynamic Light Scattering; D006860:Hydrogen Bonding; D007501:Iron / Q000737:chemistry*; D008958:Models, Molecular; D062105:Molecular Docking Simulation; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism*; D053758:Nanoparticles / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D013050:Spectrometry, Fluorescence
chemical_list: D007501:Iron; C421864:hen egg lysozyme; D009113:Muramidase