Biophysical, docking, and cellular studies on the effects of cerium oxide nanoparticles on blood components: in vitro

被引:14
作者
Eskandari, Neda [1 ]
Babadaei, Mohammad Mahdi Nejadi [1 ]
Nikpur, Sanaz [2 ]
Ghasrahmad, Ghazal [2 ]
Attar, Farnoosh [3 ]
Heshmati, Masoumeh [1 ]
Akhtari, Keivan [4 ]
Sorkhabadi, Seyed Mahdi Rezayat [5 ]
Mousavi, Seyyedeh Elaheh [5 ]
Falahati, Mojtaba [6 ]
机构
[1] Islamic Azad Univ IAUPS, Dept Cellular & Mol Biol, Fac Adv Sci & Technol, Pharmaceut Sci Branch, Tehran, Iran
[2] Islamic Azad Univ IAUPS, Dept Toxicol & Pharmacol, Fac Pharm, Pharmaceut Sci Branch, Tehran, Iran
[3] Standard Res Inst SRI, Dept Biol, Fac Food Ind & Agr, Karaj, Iran
[4] Univ Kurdistan, Dept Phys, Sanandaj, Iran
[5] Univ Tehran Med Sci, Sch Med, Dept Pharmacol, POB 13145784, Tehran, Iran
[6] Islamic Azad Univ IAUPS, Pharmaceut Sci Branch, Dept Nanotechnol, Fac Adv Sci & Technol, Tehran, Iran
关键词
cerium oxide nanoparticles; human hemoglobin; fluorescence spectroscopy; thermodynamic; circular dichroism spectroscopy; docking; flow cytometry; WALLED CARBON NANOTUBES; JOINT ALGAL TOXICITY; HUMAN SERUM-ALBUMIN; MOLECULAR DOCKING; OXIDATIVE STRESS; HEMOGLOBIN; BINDING; CELLS; PROTEIN; CYTOTOXICITY;
D O I
10.2147/IJN.S172162
中图分类号
TB3 [工程材料学];
学科分类号
0805 ; 080502 ;
摘要
Introduction: The application of nanoparticles (NPs) in medicine and biology has received great interest due to their novel features. However, their adverse effects on the biological system are not well understood. Materials and methods: This study aims to evaluate the effect of cerium oxide nanoparticles (CNPs) on conformational changes of human hemoglobin (HHb) and lymphocytes by different spectroscopic (intrinsic and synchronous fluorescence spectroscopy and far and near circular dichroism [CD] spectroscopy), docking and cellular (MTT and flow cytometry) investigations. Results and discussion: Transmission electron microscopy (TEM) showed that CNP diameter is similar to 30 nm. The infrared spectrum demonstrated a strong band around 783 cm(-1) corresponding to the CNP stretching bond. Fluorescence data revealed that the CNP is able to quench the intrinsic fluorescence of HHb through both dynamic and static quenching mechanisms. The binding constant (K-b), number of binding sites (n), and thermodynamic parameters over three different temperatures indicated that hydrophobic interactions might play a considerable role in the interaction of CNPs with HHb. Synchronous fluorescence spectroscopy indicated that microenvironmental changes around Trp and Tyr residues remain almost unchanged. CD studies displayed that the regular secondary structure of HHb had no significant changes; however, the quaternary structure of protein is subjected to marginal structural changes. Docking studies showed the larger CNP cluster is more oriented toward experimental data, compared with smaller counterparts. Cellular assays revealed that CNP, at high concentrations (>50 mu g/mL), initiated an antiproliferative response through apoptosis induction on lymphocytes. Conclusion: The findings may exhibit that, although CNPs did not significantly perturb the native conformation of HHb, they can stimulate some cellular adverse effects at high concentrations that may limit the medicinal and biological application of CNPs. In other words, CNP application in biological systems should be done at low concentrations.
引用
收藏
页码:4575 / 4589
页数:15
相关论文
共 52 条
[1]   Binding of Janus kinase inhibitor tofacitinib with human serum albumin: multi-technique approach [J].
Abdelhameed, Ali S. ;
Alam, Parvez ;
Khan, Rizwan Hasan .
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 2016, 34 (09) :2037-2044
[2]   Investigating the Interaction of Fe Nanoparticles with Lysozyme by Biophysical and Molecular Docking Studies [J].
Aghili, Zahra ;
Taheri, Saba ;
Zeinabad, Hojjat Alizadeh ;
Pishkar, Leila ;
Saboury, Ali Akbar ;
Rahimi, Arash ;
Falahati, Mojtaba .
PLOS ONE, 2016, 11 (10)
[3]   Interaction of new kinase inhibitors cabozantinib and tofacitinib with human serum alpha-1 acid glycoprotein. A comprehensive spectroscopic and molecular Docking approach [J].
Ajmal, Mohammad Rehan ;
Abdelhameed, Ali Saber ;
Alam, Parvez ;
Khan, Rizwan Hasan .
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY, 2016, 159 :199-208
[4]   Probing the conformational changes and peroxidase-like activity of cytochrome c upon interaction with iron nanoparticles [J].
Azad, Vida Jafari ;
Kasravi, Shahab ;
Zeinabad, Hojjat Alizadeh ;
Aval, Mehri Memar Bashi ;
Saboury, Ali Akbar ;
Rahimi, Arash ;
Falahati, Mojtaba .
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 2017, 35 (12) :2565-2577
[5]   Cerium oxide nanoparticles protects against acrylamide induced toxicity in HepG2 cells through modulation of oxidative stress [J].
Azari, Aala ;
Shokrzadeh, Mohammad ;
Zamani, Ehsan ;
Amani, Nahid ;
Shaki, Fatemeh .
DRUG AND CHEMICAL TOXICOLOGY, 2019, 42 (01) :54-59
[6]   TiO2, CeO2 and ZnO nanoparticles and modulation of the degranulation process in human neutrophils [J].
Babin, Kim ;
Antoine, Francis ;
Goncalves, David Miguel ;
Girard, Denis .
TOXICOLOGY LETTERS, 2013, 221 (01) :57-63
[7]  
Bailey ZS, J NEUROTRAUMA
[8]  
Basak Pijush, 2016, [Frontiers in Biology, 生物学前沿], V11, P32
[9]   An integrated approach with experimental and computational tools outlining the cooperative binding between 2-phenylchromone and human serum albumin [J].
Caruso, Icaro Putinhon ;
Barbosa Filho, Jose Maria ;
de Araujo, Alexandre Suman ;
de Souza, Fatima Pereira ;
Fossey, Marcelo Andres ;
Cornelio, Marinonio Lopes .
FOOD CHEMISTRY, 2016, 196 :935-942
[10]   Binding of fluorescent acridine dyes acridine orange and 9-aminoacridine to hemoglobin: Elucidation of their molecular recognition by spectroscopy, calorimetry and molecular modeling techniques [J].
Chatterjee, Sabyasachi ;
Kumar, Gopinatha Suresh .
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY, 2016, 159 :169-178