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Research Article | Open Access

Evaluation of the Structure and Conformation of Albumin Protein After Interaction with Graphene and Graphene Oxide

Hossein Arzani1, Fatemeh Ramezani2( )
Department of Medical Physics and Biomedical Engineering, Shahid Beheshti University of Medical Sciences, Tehran, Iran
Physiology Research Center, Iran University of Medical Sciences, Tehran, Iran
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Abstract

Given the increasing demand for graphene-based nanomaterials, it seems necessary to study their effects on the biomolecules they encounter. In this study, we will present the results of our computational study on the influence of graphene and graphene oxide (GO) on albumin. The interaction between albumin, graphene and GO was investigated using molecular dynamics and GROMACS software for 100 ns with a TIP3P water model. Binding energy, its root-mean-square deviation and structural changes were calculated. The molecular dynamics results show that the interaction of albumin with both graphene and GO structures causes changes in protein structure and that GO has a larger effect on the secondary structure. The results show that the binding energy between albumin and graphene is higher than that of GO. The analysis shows that it is more related to non-polar or hydrophobic interactions in the albumin-graphene interaction. Graphene and GO affect the protein microenvironment and reduce the amount of secondary structure, but in general the degree of change depends on the ratio of graphene or GO to albumin, GO functional groups, temperature and pH.

Keywords

InteractionGrapheneAlbuminGraphene oxid (GO)Secondary structure

References

[1]

Z. Behroozi, B. Rahimi, M.R. Hamblin, et al. Injection of cerium oxide nanoparticles to treat spinal cord injury in rats. Journal of Neuropathology & Experimental Neurology, 2022, 81: 635–642. https://doi.org/10.1093/jnen/nlac026
Crossref Google Scholar
[2]

Z. Sharifiaghdam, F. Dalouchi, M. Sharifiaghdam, et al. Curcumin-coated gold nanoparticles attenuate doxorubicin-induced cardiotoxicity via regulating apoptosis in a mouse model. Clinical and Experimental Pharmacology and Physiology, 2022, 49: 70–83. https://doi.org/10.1111/1440-1681.13579
Crossref Google Scholar
[3]

Z.S. Hoseini, A. Hajizade, A.J. Easton, et al. A meta-analysis of the efficiency of metal nanoparticles in vaccine delivery against infectious disease. Nanomedicine, 2021, 16: 481–495. https://doi.org/10.2217/nnm-2020-0358
Crossref Google Scholar
[4]

K. Zamani, N. Allah-Bakhshi, F. Akhavan, et al. Antibacterial effect of cerium oxide nanoparticle against Pseudomonas aeruginosa. BMC Biotechnology, 2021, 21: 68. https://doi.org/10.1186/s12896-021-00727-1
Crossref Google Scholar
[5]
A. Janzadeh, M.R. Hamblin, N. Janzadeh, et al. The toxic effect of silver nanoparticles on nerve cells: A systematic review and meta-analysis. Reviews of EnvironmentalContamination and Toxicology. Cham: Springer, 2021: 93–119. https://doi.org/10.1007/398_2021_67
Crossref
[6]

A. Janzadeh, Z. Behroozi, F. Saliminia, et al. Neurotoxicity of silver nanoparticles in the animal brain: A systematic review and meta-analysis. Forensic Toxicology, 2022, 40: 49–63. http://dx.doi.org/10.1007/s11419-021-00589-4
Crossref Google Scholar
[7]

Z. Behroozi, B. Rahimi, K. Kookli, et al. Distribution of gold nanoparticles into the brain: A systematic review and meta-analysis. Nanotoxicology, 2021, 15: 1059–1072. https://doi.org/10.1080/17435390.2021.1966116
Crossref Google Scholar
[8]

F. Ramezani, F. Nasirinezhad, N. Abotaleb. A review of nanotechnology strategies for neuron regeneration after spinal cord injury. Journal of Medical Physiology, 2016, 1(2): 42–54. http://jphysiology.com/index.php/jmp/article/view/9/8
Google Scholar
[9]

A.N. Banerjee. Graphene and its derivatives as biomedical materials: Future prospects and challenges. Interface Focus, 2018, 8: 20170056. https://doi.org/10.1098/rsfs.2017.0056
Crossref Google Scholar
[10]
P.V. Shinde, M. Saxena, M.K. Singh. Recent developments in graphene-based two-dimensional heterostructures for sensing applications. Fundamentalsand Sensing Applications of 2D Materials. Amsterdam: Elsevier, 2019: 407–436. https://doi.org/10.1016/b978-0-08-102577-2.00011-7
Crossref
[11]

X.M. Li, L. Tao, Z.F. Chen, et al. Graphene and related two-dimensional materials: Structure-property relationships for electronics and optoelectronics. Applied Physics Reviews, 2017, 4: 021306. http://dx.doi.org/10.1063/1.4983646
Crossref Google Scholar
[12]

J.P. Nicholson, M.R. Wolmarans, G.R. Park. The role of albumin in critical illness. British Journal of Anaesthesia, 2000, 85: 599–610. https://doi.org/10.1093/bja/85.4.599
Crossref Google Scholar
[13]

T.R. Figueira, A.E. Vercesi, H.C.F. Oliveira. Lack of plasma albumin impairs intravascular lipolysis and explains the associated free fatty acids deficiency and hypertriglyceridemia. Lipids in Health and Disease, 2010, 9: 146. https://doi.org/10.1186/1476-511x-9-146
Crossref Google Scholar
[14]

D.G. Levitt, M.D. Levitt. Human serum albumin homeostasis: A new look at the roles of synthesis, catabolism, renal and gastrointestinal excretion, and the clinical value of serum albumin measurements. International Journal of General Medicine, 2016, 9: 229–255. https://doi.org/10.2147/ijgm.s102819
Crossref Google Scholar
[15]

S. Walayat, D. Martin, J. Patel, et al. Role of albumin in cirrhosis: From a hospitalist's perspective. Journal of Community Hospital Internal Medicine Perspectives, 2017, 7: 8–14. https://doi.org/10.1080/20009666.2017.1302704
Crossref Google Scholar
[16]

F. Ramezani, H. Rafii-Tabar. An in-depth view of human serum albumin corona on gold nanoparticles. Molecular Bio Systems, 2015, 11: 454–462. http://dx.doi.org/10.1039/C4MB00591K
Crossref Google Scholar
[17]

F. Ramezani, M. Amanlou, H. Rafii-Tabar. Gold nanoparticle shape effects on human serum albumin corona interface: A molecular dynamic study. Journal of Nanoparticle Research, 2014, 16: 2512. http://dx.doi.org/10.1007/s11051-014-2512-1
Crossref Google Scholar
[18]

S.H. Li, A.N. Aphale, I.G. Macwan, et al. Graphene oxide as a quencher for fluorescent assay of amino acids, peptides, and proteins. ACS Applied Materials & Interfaces, 2012, 4: 7069–7075. https://doi.org/10.1021/am302704a
Crossref Google Scholar
[19]

R. Feng, Y.P. Yu, C.X. Shen, et al. Impact of graphene oxide on the structure and function of important multiple blood components by a dose-dependent pattern. Journal of Biomedical Materials Research Part A, 2015, 103: 2006–2014. https://doi.org/10.1002/jbm.a.35341
Crossref Google Scholar
[20]

F. Ramezani. Effects of orientation on the stability and affinity of antibody-GNP conjugation. The Protein Journal, 2019, 38: 134–141. http://dx.doi.org/10.1007/s10930-019-09812-z
Crossref Google Scholar
[21]

S. Hashemzadeh, F. Ramezani, H. Rafii-Tabar. Study of molecular mechanism of the interaction between MEK1/2 and trametinib with docking and molecular dynamic simulation. Interdisciplinary Sciences: Computational Life Sciences, 2019, 11: 115–124. http://dx.doi.org/10.1007/s12539-018-0305-4
Crossref Google Scholar
[22]

F. Ramezani, M. Habibi, H. Rafii-Tabar, et al. Effect of peptide length on the conjugation to the gold nanoparticle surface: A molecular dynamic study. DARU Journal of Pharmaceutical Sciences, 2015, 23: 9. http://dx.doi.org/10.1186/s40199-014-0085-2
Crossref Google Scholar
[23]

M. Vahed, F. Ramezani, V. Tafakori, et al. Molecular dynamics simulation and experimental study of the surface-display of SPA protein via Lpp-OmpA system for screening of IgG. AMB Express, 2020, 10: 161. http://dx.doi.org/10.1186/s13568-020-01097-1
Crossref Google Scholar
[24]

M. Abbasi, F. Ramezani, M. Elyasi, et al. A study on quantitative structure-activity relationship and molecular docking of metalloproteinase inhibitors based on L-tyrosine scaffold. DARU Journal of Pharmaceutical Sciences, 2015, 23: 29. http://dx.doi.org/10.1186/s40199-015-0111-z
Crossref Google Scholar
[25]

X.X. Ba, T. Gao, M. Yang, et al. Thermodynamics of the interaction between graphene quantum dots with human serum albumin and γ-globulins. Journal of Solution Chemistry, 2020, 49: 100–116. http://dx.doi.org/10.1007/s10953-019-00941-8
Crossref Google Scholar
[26]

Z.J. Ding, H.W. Ma, Y.Y. Chen. Interaction of graphene oxide with human serum albumin and its mechanism. RSC Advances, 2014, 4: 55290–55295. http://dx.doi.org/10.1039/C4RA09613D
Crossref Google Scholar
[27]

Z.J. Ding, Z.J. Zhang, H.W. Ma, et al. In vitro hemocompatibility and toxic mechanism of graphene oxide on human peripheral blood T lymphocytes and serum albumin. ACS Applied Materials & Interfaces, 2014, 6: 19797–19807. https://doi.org/10.1021/am505084s
Crossref Google Scholar
[28]

S. Huang, H. Qiu, S. Lu, et al. Study on the molecular interaction of graphene quantum dots with human serum albumin: Combined spectroscopic and electrochemical approaches. Journal of Hazardous Materials, 2015, 285: 18–26. http://dx.doi.org/10.1016/j.jhazmat.2014.11.019
Crossref Google Scholar
[29]

A. Khan, F. Khan, M. Shahwan, et al. Mechanistic insight into the binding of graphene oxide with human serum albumin: Multispectroscopic and molecular docking approach. Spectrochim. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 2021, 256: 119750. https://doi.org/10.1016/j.saa.2021.119750
Crossref Google Scholar
[30]

H. Lee, M.H. Tran, H.K. Jeong, et al. Nonspecific cleavage of proteins using graphene oxide. Analytical Biochemistry, 2014, 451: 31–34. https://doi.org/10.1016/j.ab.2014.01.017
Crossref Google Scholar
[31]

X. Liu, C. Yan, K.L. Chen. Adsorption of human serum albumin on graphene oxide: Implications for protein Coronaformation and conformation. Environmental Science & Technology, 2019, 53: 8631–8639. https://doi.org/10.1021/acs.est.8b03451
Crossref Google Scholar
[32]

Z.Z. Nan, C.C. Hao, X.Q. Ye, et al. Interaction of graphene oxide with bovine serum albumin: A fluorescence quenching study. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 2019, 210: 348–354. https://doi.org/10.1016/j.saa.2018.11.028
Crossref Google Scholar
[33]

Šimšíková M. Interaction of graphene oxide with albumins: Effect of size, pH, and temperature. Archives of Biochemistry and Biophysics, 2016, 593: 69–79. http://dx.doi.org/10.1016/j.abb.2016.02.015
Crossref Google Scholar
[34]

B.B. Sun, Y.Q. Zhang, W. Chen, et al. Concentration dependent effects of bovine serum albumin on graphene oxide colloidal stability in aquatic environment. Environmental Science & Technology, 2018, 52: 7212–7219. https://doi.org/10.1021/acs.est.7b06218
Crossref Google Scholar
[35]

Y. Sun, J.L. Ding, H. Zong, et al. Molecular dynamics simulations of albumin and graphene structures and their interaction. Journal of Southeast University (Natural Science Edition), 2014, 44: 123–128. http://dx.chinadoi.cn/10.3969/j.issn.1001-0505.2014.01.022
Crossref Google Scholar
[36]

P. Hampitak, D. Melendrez, M. Iliut, et al. Protein interactions and conformations on graphene-based materials mapped using a quartz-crystal microbalance with dissipation monitoring (QCM-D). Carbon, 2020, 165: 317–327. https://doi.org/10.1016/j.carbon.2020.04.093
Crossref Google Scholar
Nano Biomedicine and Engineering
Volume 14 Issue 4,
December 2022
Pages 375-384
DOI: 10.5101/nbe.v14i4.p375-384
Cite this article:
Arzani H, Ramezani F. Evaluation of the Structure and Conformation of Albumin Protein After Interaction with Graphene and Graphene Oxide. Nano Biomedicine and Engineering, 2022, 14(4): 375-384. https://doi.org/10.5101/nbe.v14i4.p375-384

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Received: 07 September 2022
Revised: 02 December 2022
Accepted: 22 December 2022
Published: 31 December 2022
© Hossein Arzani and Fatemeh Ramezani.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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