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Research Article | Open Access

Interaction of Colloidal Gold Nanoparticles with Protein

Department of Chemistry, Faculty of Science, University of Kufa, Najf, Iraq
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Abstract

The interaction between nanoparticles (NPs) with biomaterials has many applications. In the present research, the interaction between colloidal gold nanoparticles and human protein, human chorionic gonadotropin (hCG) was studied to find out the changes in the structure of protein at the presence of colloidal gold nanoparticles and the quantity of protein that colloidal gold nanoparticles absorbed on the hCG surface. Colloidal gold nanoparticles were synthesized through the reduction of HAuCl4 using ammonium hydroxide. The gold nanoparticles were estimated at 20 nm in diameter. The results showed that there was a significant adsorption of colloidal gold nanoparticles absorbed on the hCG surface. Sips equation was used to express the absorption of isotherms and to calculate the absorption parameters and thermodynamic constant. Fluorescence study indicated a mild change in the tertiary structure near the microenvironment of the aromatic amino acids tyrosine and phenyl alanine, which was due to the interaction forces between the colloidal gold nanoparticles and hCG protein that affected the environment. It can be concluded that the colloidal gold nanoparticles had effects on the tertiary structure of proteins and affected the availability of hCG concentration.

References

[1]

A. Albanese, P.S. Tang, and W.C.W. Chan, The effect of nanoparticle size, shape, and surface chemistry on biological systems. Annu. Rev. Biomed. Eng., 2012, 14: 1-16.

[2]

S. Swain, Nanoparticles for cancer targeting: Current and future directions. Curr Drug Deliv., 2016, 13(8): 1290-1302.

[3]

X.L. Loh, Utilising inorganic nanocarriers for gene delivery. Biomat. Sci., 2016, 4(1): 70-86.

[4]

A.R. Fernandes, Multifunctional gold-nanoparticles: A nanovectorization tool for the targeted delivery of novel chemotherapeutic agents. J. Contr. Release, 2017, 245: 52-61.

[5]

M.A. Safwat, Gold nanoparticles enhance 5-fluorouracil anticancer efficacy against colorectal cancer cells. Inter. J. Pharmaceutics, 2016, 513(1–2): 648-658.

[6]

Z. Li, Recent advances of using hybrid nanocarriers in remotely controlled therapeutic delivery. Small, 2016, 12(35): 4782-4806.

[7]

E. Engel, A. Michiardi, M. Navarro, et al., Nanotechnology in regenerative medicine: the materials side. Trends Biotechnol., 2008, 26: 39-47.

[8]

A. Patzelt, Do nanoparticles have a future in dermal drug delivery? J. Contr. Release, 2017, 246: 174-182.

[9]

W. Zhang, pH and near-infrared light dual-stimuli responsive drug delivery using DNA-conjugated gold nanorods for effective treatment of multidrug resistant cancer cells. J. Contr. Release, 2016, 232: 9-19.

[10]

E. Ye, An experimental and theoretical investigation of the anisotropic branching in gold nanocrosses. Nanoscale, 2016, 8(1): 543-552.

[11]

R. Shukla, Biocompatibility of gold nanoparticles and their endocytotic fate inside the cellular compartment: a microscopic overview. Langmuir, 2005, 21(23): 10644-10654.

[12]

D. Gidaspow, V. Jiradilok, Nanoparticle gasifier fuel cell for sustainable energy future. J Power Source, 2007, 166: 400-410.

[13]

I.L. Medintz, H.T. Uyeda, E.R. Goldman, et al. Quantum dot bioconjugates for imaging, labeling and sensing. Nat Mater., 2005, 4: 435-446.

[14]

C. Corot. P. Robert, J.M. Idée, et al., Recent advances in iron oxide nanocrystal technology for medical imaging. Adv. Drug Deliv. Rev., 2006, 58: 1471–1504.

[15]

K. Huang, Q. Dou, X.J. Loh, Nanomaterial mediated optogenetics: opportunities and challenges. RSC Advances, 2016, 6(65): 60896-60906.

[16]

M.M. Teo, D.J. Young, and X.J. Loh, Magnetic anisotropic particles: Toward remotely actuated applications. Part. Part. Sys. Char., 2016, 33(10): 709-728.

[17]

D.M. Mariagrazia, S. Shaharum, and A.R. Khairunisak, Overview of the main methods used to combine proteins with nanosystems: absorption, bioconjugation, and encapsulation. Inter. J. Nanomed., 2010, 5: 37-49

[18]

B. Steven, K. Galina, and O. John, Metabolism of hCG and hLH to multiple urinary forms. Mol. Cellular Endocrinol., 1996, 125: 121-131.

[19]

G. Kovalevskaya, O. Genbacev, and S.R. Fisher, Trophoblast origin of hCG isoforms: cytotrophoblasts are the primary source of choriocarcinoma-like hCG. Mol. Cellular Endocrinol., 2002, 194: 147-155.

[20]

O.P. Bahl, R.B. Carlsen, Human chorionic gonadotrophin: Amino acid sequences of the α and β subunits. J Biol Chem., 1975, 250: 5247-5253.

[21]

F.J. Morgan, S. Birken, and R.E. Canfield, The amino acid sequence of human chorionic gonadotropin. The α-subunit and the β- subunit. Endocrinology, 1975, 250: 5247-5255.

[22]

L.A. Cole, Biological functions of hCG and hCG-related Molecules. Cole Reproductive Biolo. Endocrinology, 2010, 8: 102-112.

[23]

C. Stock, S.F. Pedersen, Roles of pH and the Na+/H+ exchanger NHE1 in cancer: From cell biology and animal models to an emerging translational perspective? Semin Cancer Biol., 2017, 43: 5-16.

[24]

K. Shameli, M.B. Ahmad, P. Shabanzadeh, et al., Effect of Curcuma longa tuber powder extract on size of silver nanoparticles prepared by green method. Res. Chem. Intermed., 2014, 40 (3): 1313-1325.

[25]

I. Lynch, C.T. edervall, M. Lundqvist, et al., The nanoparticle-protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century. Adv. Colloid Interface Sci., 2007, 134–135: 167-174.

[26]

K. Shameli, M.B. Ahmad, EAJ Al-Mulla, et al., Antibacterial effect of silver nanoparticles on talc composites. Res. Chem. Intermed., 2015, 41(1): 251-263.

[27]

Z. Zhang, Y. Zhang, Method of calculating the thermodynamic parameters from some isothermal absorption models. Acta of Northwest Sci-Tech University of Agriculture and Forestry, 1998, 26(2): 94-98.

[28]

A.J. Haider, M.R. Mohammed, Synthesis of silver nanoparticle decorated carbon nanotubes and its antimicrobial activity against growth of bacteria. Rendiconti Lincei, 2014, 25(3): 403-407.

[29]

M. Epple, K. Ganesan, R. Heumann R., Klesing at al., Application of calcium phosphate nanoparticles in biomedicine, J. Mater. Chem., 2010, 20: 18–23.

[30]

P. Neogi, J.C. Wang, Stability of two-dimensional growth of a packed body of proteins on a solid surface. Langmuir, 2011, 9: 5347-553.

[31]

S. Umoren, U. Etim, A. Israel, Adsorption of methylene blue from industrial effluent using poly (vinyl alcohol). Mater J. Environ. Sci., 2013, 4(1): 75-86.

[32]

L. Wang, W. Zhao, W. Tan, Bioconjugated silica nanoparticles: Development and applications. Nano Res., 2008, 1: 99-115.

[33]

Q. Liu, T. Zheng, Equilibrium isotherms and kinetics modeling of methylene blue adsorption on agricultural wastes-based activated carbons. Surf. Sci., 2010, 256: 3309-3315.

[34]

P. Kumar, S. Ramalingam, and K. Sathishkumar, Adsorption characteristics of methylene blue onto the N-succinyl-chitosan-g-polyacrylamide/attapulgite composite. Chem. Eng., 2011, 28: 149–155.

[35]

J. Toth, Adsorption: theory, modeling, and analysis Surfactant, Marcel Dekker, Sci. Ser., 2002, 107(50): 971-983.

[36]

M. De, S. Rana, and V.M. Rotello, Nickel-ion-mediated control of the stoichiometry of His-tagged protein/nanoparticle interactions. Macromol. Biosci., 2009, 9: 174-178.

[37]

S. Vaitheeswaran, A. Garcia, Protein stability at a carbon nanotube interface. J. Chem. Phys., 2011, 134: 12-24.

[38]

S. Mitragotri, J. Lahann, Physical approaches to biomaterial design. Nature Mater., 2009, 8: 15-23.

[39]

Z. Adamczyk, J. Barbasz, and M. Cieśla, Mechanisms of fibrinogen adsorption at solid substrates. Langmuir, 2011, 27(11): 6868-6878.

[40]

M.R. Eftink, Methods of biochemical analysis. John Wiley, NY, 1991: 127-205.

[41]

J.R. Lakowicz, Principles of fluorescence spectroscopy. Kluwer-Plenum, NY, 1999: 69-71.

Nano Biomedicine and Engineering
Pages 298-305
Cite this article:
Radhi SW. Interaction of Colloidal Gold Nanoparticles with Protein. Nano Biomedicine and Engineering, 2017, 9(4): 298-305. https://doi.org/10.5101/nbe.v9i4.p298-305

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Received: 02 November 2017
Accepted: 28 November 2017
Published: 25 December 2017
© Sami Waheed Radhi.

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

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