BSA-drug-ZnO-PEI conjugates interaction with glycans of gp60 endothelial cell receptor protein for targeted drug delivery: a comprehensive spectroscopic study

References

• Abbasi, S., Paul, A., & Prakash, S. (2011). Investigation of siRNA loaded PEI-coated HAS NPs complexes for the treatment of breast cancer. Cell Biochemistry and Biophysics, 61(2), 277–287. https://doi.org/10.1007/s12013-011-9201-9
   PubMed Web of Science ®Google Scholar
• Altunbek, M., Keleştemur, S., Baran, G., & Çulha, M. (2018). Role of modification route for zinc oxide nanoparticles on protein structure and their effects on glioblastoma cells. International Journal of Biological Macromolecules, 118(Pt A), 271–278. https://doi.org/10.1016/j.ijbiomac.2018.06.059
   PubMedGoogle Scholar
• Asani, S. C., Umrani, R. D., & Paknikar, K. M. (2016). In vitro studies on the pleotropic antidiabetic effects of zinc oxide nanoparticles. Nanomedicine (London, England), 11(13), 1671–1687. https://doi.org/10.2217/nnm-2016-0119
   PubMed Web of Science ®Google Scholar
• Bardhan, M., Mandal, G., & Ganguly, T. (2009). Steady state, time resolved, and circular dichroism spectroscopic studies to reveal the nature of interactions of zinc oxide nanoparticles with transport protein bovine serum albumin and to monitor the possible protein conformational changes. Journal of Applied Physics, 106(3), 034701–0347015. https://doi.org/10.1063/1.3190483
   Web of Science ®Google Scholar
• Beyth, N., Houri-Haddad, Y., Baraness-Hadar, L., Yudovin-Farber, I., Domb, A. J., & Weiss, E. I. (2008). Surface antimicrobial activity and biocompatibility of incorporated polyethylenimine nanoparticles. Biomaterials, 29(31), 4157–4163. − https://doi.org/10.1016/j.biomaterials.2008.07.003
   PubMed Web of Science ®Google Scholar
• Bhadra, P., Mitra, M. K., Das, G. C., Dey, R., & Mukherjee, S. (2011). Interaction of chitosan capped ZnO nanorods with Escherichia coli. Materials Science and Engineering: C, 31(5), 929–937. https://doi.org/10.1016/j.msec.2011.02.015
   Web of Science ®Google Scholar
• Bhogale, A., Patel, N., Sarpotdar, P., Mariam, J., Dongre, P. M., Miotello, A., & Kothari, D. C. (2013). Systematic investigation on the interaction of bovine serum albumin with ZnO nanoparticles using fluorescence spectroscopy. Colloids and Surfaces. B, Biointerfaces, 102, 257–264. https://doi.org/10.1016/j.colsurfb.2012.08.023
   PubMed Web of Science ®Google Scholar
• Bian, S. W., Mudunkotuwa, I. A., Rupasinghe, T., & Grassian, V. H. (2011). Aggregation and dissolution of 4 nm ZnO nanoparticles in aqueous environments: Influence of pH, ionic strength, size, and adsorption of humic Acid. Langmuir : The ACS Journal of Surfaces and Colloids, 27(10), 6059–6068. https://doi.org/10.1021/la200570n
   PubMed Web of Science ®Google Scholar
• Brayner, R., Ferrari-Iliou, R., Brivois, N., Djediat, S., Benedetti, M. F., & Fiévet, F. (2006). Toxicological impact studies based on Escherichia coli bacteria in ultrafine ZnO nanoparticles colloidal medium. Nano Letters, 6(4), 866–870. https://doi.org/10.1021/nl052326h
   PubMed Web of Science ®Google Scholar
• Bruchez, M. J., Moronne, M., Gin, P., Weiss, S., & Alivisatos, A. P. (1998). Semiconductor nanocrystals as fluorescent biological labels. Science (New York, N.Y.), 281(5385), 2013–2016. https://doi.org/10.1126/science.281.5385.2013
   PubMed Web of Science ®Google Scholar
• Chakraborti, S., Chatterjee, T., Joshi, P., Poddar, A., Bhattacharyya, B., Singh, S. P., Gupta, V., & Chakrabarti, P. (2010). Structure and activity of lysozyme on binding to ZnO nanoparticles. Langmuir : The ACS Journal of Surfaces and Colloids, 26(5), 3506–3513. https://doi.org/10.1021/la903118c
   PubMed Web of Science ®Google Scholar
• Chakraborti, S., Joshi, P., Chakravarty, D., Shanker, V., Ansari, Z. A., Singh, S. P., & Chakrabarti, P. (2012). Interaction of Polyethyleneimine-Functionalized ZnO Nanoparticles with bovine serum albumin. Langmuir : The ACS Journal of Surfaces and Colloids, 28(30), 11142–11152. https://doi.org/10.1021/la3007603
   PubMed Web of Science ®Google Scholar
• Chithrani, B. D., Ghazani, A. A., & Chan, W. C. (2006). Determining the size and shape dependence of gold nanoparticle uptake into mammalian cells. Nano Letters, 6(4), 662–668. https://doi.org/10.1021/nl052396o
   PubMed Web of Science ®Google Scholar
• Comenge, J., Sotelo, C., Romero, F., Gallego, O., Barnadas, A., Parada, T. G., Domínguez, F., & Puntes, V. F. (2012). Detoxifying antitumoral drugs via nanoconjugation: The case of gold nanoparticles and cisplatin. PLoS One, 7(10), e47562. https://doi.org/10.1371/journal.pone.0047562
   PubMed Web of Science ®Google Scholar
• De, M., Ghosh, P. S., & Rotello, V. M. (2008). Applications of Nanoparticles in Biology. Advanced Materials, 20(22), 4225–4241. https://doi.org/10.1002/adma.200703183
   Web of Science ®Google Scholar
• Desai, N. (2015). Nanoparticle albumin-bound anticancer agents. Advances in the Pharmaceutical Sciences Series, 20, 329–354.
   Google Scholar
• Dingari, N. C., Horowitz, G. L., Kang, J. W., Dasari, R. R., & Barman, I. (2012). Raman Spectroscopy provides a powerful diagnostic tool for accurate determination of albumin glycation. Plos One, 7(2), e32406. https://doi.org/10.1371/journal.pone.0032406
   PubMed Web of Science ®Google Scholar
• EFSA CEF Panel On food contact materials, EU, flavourings and processing aids. (2015). Scientific Opinion on the safety evaluation of the substance zinc oxide, nanoparticles, uncoated and coated with [3-(methacryloxy) propyl] trimethoxysilane, for use in food contact materials. EFSA Journal., 13, 4063–4072.
   Web of Science ®Google Scholar
• Elzoghby, A. O., Samy, W. M., & Elgindy, N. A. (2012). Albumin-based nanoparticles as potential controlled release drug delivery systems. Journal of Controlled Release : Official Journal of the Controlled Release Society, 157(2), 168–182. https://doi.org/10.1016/j.jconrel.2011.07.031
   PubMed Web of Science ®Google Scholar
• Ferrari, M. (2005). Nature Review Cancer nanotechnology: Opportunities and challenges. Cancer, 5, 161–171.
   PubMed Web of Science ®Google Scholar
• Han, H., Wang, J., Chen, T., Yin, L., Jin, Q., & Ji, J. (2017). Enzyme-sensitive gemcitabine conjugated albumin nanoparticles as a versatile theranostic nanoplatform for pancreatic cancer treatment. Journal of Colloid and Interface Science, 507, 217–224. https://doi.org/10.1016/j.jcis.2017.07.047
   PubMed Web of Science ®Google Scholar
• Harada, I., & Takeuchi, H. (1986). Raman and ultraviolet resonance Raman of proteins and related compounds. Spectroscopy of Biological Systems, 13, 113–175.
   Google Scholar
• Hassanian, M., Aryapour, H., Goudarzi, A., & Javan, M. B. (2021). Are zinc oxide nanoparticles safe? A structural study on human serum albumin using in vitro and in silico methods. Journal of Biomolecular Structure and Dynamics, 39(1), 330–333. https://doi.org/10.1080/07391102.2019.1711189
   PubMed Web of Science ®Google Scholar
• Jahanban-Esfahlan, A., & Panahi-Azar, V. (2016). Interaction of glutathione with bovine serum albumin: Spectroscopy and molecular docking. Food Chemistry, 202, 426–431. https://doi.org/10.1016/j.foodchem.2016.02.026
   PubMed Web of Science ®Google Scholar
• Jahanban-Esfahlan, A., Panahi-Azar, V., & Sajedi, S. (2015). Spectroscopic and molecular docking studies on the interaction between N-acetyl cysteine and bovine serum albumin. Biopolymers, 103(11), 638–645. https://doi.org/10.1002/bip.22697
   PubMed Web of Science ®Google Scholar
• Jones, N., Ray, B., Ranjit, K. T., & Manna, A. C. (2008). Antibacterial activity of ZnO nanoparticle suspensions on a broad spectrum of microorganisms. FEMS Microbiology Letters, 279(1), 71–76. https://doi.org/10.1111/j.1574-6968.2007.01012.x
   PubMed Web of Science ®Google Scholar
• Joshi, P., Ansari, Z., Singh, S. P., & Shanker, V. (2009). Synthesis and characterization of highly fluorescent water dispersible ZnO quantum dots. Journal of Computational and Theoretical Nanoscience, 2, 360–363.
   Google Scholar
• Joshi, P., Chakraborti, S., Chakrabarti, P., Haranath, D., Shanker, V., Ansari, Z. A., Singh, S. P., & Guptas, V. (2009). Role of surface adsorbed anionic species in antibacterial activity of ZnO quantum dots against Escherichia coli. Journal of Nanoscience and Nanotechnology, 9(11), 6427–6433. https://doi.org/10.1166/jnn.2009.1584
   PubMed Web of Science ®Google Scholar
• Kandagal, P. B., Ashoka, S., Seetharamappa, J., Shaikh, S. M. T., Jadegoud, Y., & Ijare, O. B. (2006). Study of the interaction of an anticancer drug with human and bovine serum albumin: Spectroscopic approach. Journal of Pharmaceutical and Biomedical Analysis, 14, 393–399.
   Google Scholar
• Karimi, M., Bahrami, S., Ravari, S. B., Zangabad, P. S., Mirshekari, H., Bozorgomid, M., Shahreza, S., Sori, M., & Hamblin, M. R. (2016). Albumin nanostructures as advanced drug delivery systems. Expert Opinion on Drug Delivery, 13(11), 1609–1623. https://doi.org/10.1080/17425247.2016.1193149
   PubMed Web of Science ®Google Scholar
• Karthikeyan, S., Velmurugan, D., Aruna, P. R., Ganesan, S., Tamilkumar, P., & Bharanidharan, G. (2015). Binding Studies of Cisplatin with Human Serum Albumin. Trends in Biomaterials and Artificial Organs., 29, 273–278.
   Google Scholar
• Kaszuba, M., Corbett, J., Watson, F. M., & Jones, A. (2010). High-concentration zeta potential measurements using light-scattering techniques. Philosophical Transactions. Series A, Mathematical, Physical, and Engineering Sciences, 368(1927), 4439–4451. https://doi.org/10.1098/rsta.2010.0175
   PubMed Web of Science ®Google Scholar
• Khade, B. S., Mathe, V. L., & Dongre, P. M. (2017). α-amylase binding to thermal plasma synthesized zinc oxide nanosheets: A fluorescence study. Journal of Luminescence, 187, 449–456. https://doi.org/10.1016/j.jlumin.2017.03.033
   Web of Science ®Google Scholar
• Kim, S. H., Jeong, J. H., Chun, K. W., & Park, T. G. (2005). Target-specific cellular uptake of PLGA nanoparticles coated with poly(L-lysine)-poly(ethylene glycol)-folate conjugate . Langmuir : The ACS Journal of Surfaces and Colloids, 21(19), 8852–8857. https://doi.org/10.1021/la0502084
   PubMed Web of Science ®Google Scholar
• Kratz, F. (2010). Albumin, a versatile carrier in oncology. Int. Journal of Clinical Pharmacology and Therapeutics, 48(07), 453–455. https://doi.org/10.5414/CPP48453
   PubMedGoogle Scholar
• Krause-Heuer, M., Price, W. S., & Aldrich-Wright, J. R. (2012). Spectroscopic investigations on the interactions of potent platinum(II) anticancer agents with bovine serum albumin. Journal of Chemical Biology, 5(3), 105–113. https://doi.org/10.1007/s12154-012-0074-1
   PubMedGoogle Scholar
• Kumari, N., Mathe, V. L., & Dongre, P. M. (2019). Albumin nanoparticles conjugates binding with glycan - A strategic approach for targeted drug delivery. International Journal of Biological Macromolecules, 126, 74–90. https://doi.org/10.1016/j.ijbiomac.2018.12.184
   PubMed Web of Science ®Google Scholar
• Kushwah, V., Agrawal, A. K., Dora, C. P., Mallinson, D., Lamprou, D. M., Gupta, R. C., & Jain, S. (2017). Novel gemcitabine conjugated albumin nanoparticles: A potential strategy to enhance drug efficacy in pancreatic cancer treatment. Pharmaceutical Research, 34(11), 2295–2311. https://doi.org/10.1007/s11095-017-2238-8
   PubMed Web of Science ®Google Scholar
• Lee, H. J., Lee, S. G., Oh, E. J., Chung, H. Y., Han, S. I., Kim, E. J., Seo, S. Y., Ghim, H. D., Yeum, J. H., & Choi, J. H. (2011). Antimicrobial polyethyleneimine-silver nanoparticles in a stable colloidal dispersion. Colloids and Surfaces B: Biointerfaces, 88(1), 505–511. − https://doi.org/10.1016/j.colsurfb.2011.07.041
   PubMed Web of Science ®Google Scholar
• Lee, S. Y., Huh, M. S., Lee, S., Lee, S. J., Chung, H., Park, J. H., Oh, Y. K., Choi, K., Kim, K., & Kwon, I. C. (2010). Stability and cellular uptake of polymerized siRNA (poly-siRNA)/polyethylenimine (PEI) complexes for efficient gene silencing . Journal of Controlled Release : Official Journal of the Controlled Release Society, 141(3), 339–346. https://doi.org/10.1016/j.jconrel.2009.10.007
   PubMed Web of Science ®Google Scholar
• Merlot, A. M., Kalinowski, D. S., & Richardson, D. R. (2014). Unraveling the mysteries of serum albumin—more than just a serum protein. Frontiers in Physiology, 5, 1–7. https://doi.org/10.3389/fphys.2014.00299
   PubMed Web of Science ®Google Scholar
• Neault, J. F., & Tajmir-Riahi, H. A. (1998). Interaction of cisplatin with human serum albumin. Drug binding mode and protein secondary structure. Biochimica et Biophysica Acta, 1384(1), 153–159. https://doi.org/10.1016/s0167-4838(98)00011-9
   PubMedGoogle Scholar
• Nemecek, D., Stepanek, J., & Jr., & Thomas, G. J. (2013). Raman spectroscopy of proteins and nucleoproteins. Current Protocols in Protein Science, 17, 1–52.
   Google Scholar
• Parize, R., Garnier, J. D., Appert, E., Chaix-Pluchery, O., & Consonni, V. (2018). Effects of polyethyleneimine and its molecular weight on the chemical bath deposition of ZnO nanowires. ACS Omega., 3(10), 12457–12464. https://doi.org/10.1021/acsomega.8b01641
   PubMed Web of Science ®Google Scholar
• Park, S. J., Borin, B. N., Martinez-Yamout, M. A., & Dyson, H. J. (2011). The client protein p53 adopts a molten globule-like state in the presence of Hsp90. Nature Structural & Molecular Biology, 18(5), 537–541. https://doi.org/10.1038/nsmb.2045
   PubMed Web of Science ®Google Scholar
• Prasad, A. R., Basheer, S. M., Williams, L., & Joseph, A. (2019). Highly selective inhibition of α-glucosidase by green synthesised ZnO nanoparticles - In-vitro screening and in-silico docking studies. International Journal of Biological Macromolecules, 139, 712–718. https://doi.org/10.1016/j.ijbiomac.2019.08.033
   PubMed Web of Science ®Google Scholar
• Rasmussen, J. W., Martinez, E., Louka, P., & Wingett, D. G. (2010). Zinc oxide nanoparticles for selective destruction of tumor cells and potential for drug delivery applications. Expert Opinion on Drug Delivery, 7(9), 1063–1077. https://doi.org/10.1517/17425247.2010.502560
   PubMed Web of Science ®Google Scholar
• Schnitzer, J. E., & Bravo, J. (1993). High affinity binding, endocytosis, and degradation of conformationally modified albumins, Potential role of gp30 and gp18 as novel scavenger receptors. The Journal of Biological Chemistry, 268(10), 7562–7570.
   PubMed Web of Science ®Google Scholar
• Shen, H., Gu, Z., Jian, K., & Qi, J. (2013). In vitro study on the binding of gemcitabine to bovine serum albumin. Journal of Pharmaceutical and Biomedical Analysis, 75, 86–93. https://doi.org/10.1016/j.jpba.2012.11.021
   PubMed Web of Science ®Google Scholar
• Shiryaev, M. A., Jin, Y. J., Bong, H. C., & Baranov, A. (2017). ZnO nanoparticle modification by Polyethylenimine for Biomolecule Conjugation. Nanotechnologies in Russia, 12(11-12), 613–619. https://doi.org/10.1134/S199507801706009X
   Web of Science ®Google Scholar
• Siamwiza, M. N., Lord, R. C., Chen, M. C., Takamatsu, T., Harada, I., Matsuura, H., & Shimanouchi, T. (1975). Interpretation of the doublet at 850 and 830 cm−1 in the Raman spectra of tyrosyl residues in proteins and certain model compounds. Biochemistry, 14(22), 4870–4876. https://doi.org/10.1021/bi00693a014
   PubMed Web of Science ®Google Scholar
• Sjöberg, B., Foley, S., Cardey, B., & Enescu, M. (2014). An experimental and theoretical study of the amino acid side chain Raman bands in proteins. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 128, 300–311. https://doi.org/10.1016/j.saa.2014.02.080
   PubMed Web of Science ®Google Scholar
• Sun, S. K., Wang, H. F., & Yan, X. P. (2011). A sensitive and selective resonance light scattering bioassay for homocysteine in biological fluids based on target-involved assembly of polyethyleneimine-capped Ag-nanoclusters. Chemical Communications (Cambridge, England), 47(13), 3817–3819. − https://doi.org/10.1039/c0cc04463f
   PubMed Web of Science ®Google Scholar
• Syame, S. M., Eisa, Z. M., Eltayeb, R., & Hakim, A. S. (2018). Synthesis and Characterization of Cisplatin-Loaded BSA (Bovine Serum Albumin) Nanoparticles as Drug Delivery System against Pancreatic Cancer Cells. Journal of Pharmacy, 8, 39–48.
   Google Scholar
• Tabibiazar, M., Davaran, S., Hashemi, M., Homayonirad, A., Rasoulzadeh, F., Hamishehkar, H., & Mohammadifar, M. A. (2015). Design and fabrication of a food-grade albumin-stabilized nano emulsion. Food Hydrocolloids., 44, 220–228. https://doi.org/10.1016/j.foodhyd.2014.09.005
   Web of Science ®Google Scholar
• Tauber, R., Park, C. S., & Reutter, W. (1983). Intramolecular heterogeneity of degradation in plasma membrane glycoproteins: Evidence for a general characteristic. Proceedings of the National Academy of Sciences, 80(13), 4026–4029. https://doi.org/10.1073/pnas.80.13.4026
   PubMed Web of Science ®Google Scholar
• Tiwari, V., Mishra, N., Gadani, K., Solanki, P. S., Shah, N. A., & Tiwari, M. (2018). Mechanism of anti-bacterial activity of zinc oxide nanoparticle against carbapenem-resistant acinetobacter baumannii. Frontiers in Microbiology, 6, 1–10.
   Google Scholar
• Uversky, V. N., Narizhneva, N. V., Ivanova, T. V., & Tomashevski, A. Y. (1997). Rigidity of human alpha-fetoprotein tertiary structure is under ligand control. Biochemistry, 36(44), 13638–13645. https://doi.org/10.1021/bi970332p
   PubMed Web of Science ®Google Scholar
• Verma, A., & Stellacci, E. (2010). Effects of surface properties on nanoparticles cell interaction. Small, 6(1), 12–21. https://doi.org/10.1002/smll.200901158
   PubMed Web of Science ®Google Scholar
• Vicentini, D. S., Jr Smania, A., & Laranjeira, M. C. M. (2010). Chitosan/poly (vinyl alcohol) films containing ZnO nanoparticles and plasticizers. Materials Science and Engineering: C, 30(4), 503–508. https://doi.org/10.1016/j.msec.2009.01.026
   Web of Science ®Google Scholar
• Wang, L., Liang, T., Ma, J., Sun, L., Yang, C., Meng, L., Liang, T., & Li, Q. (2020). Effects of nanoparticle size on the interaction between zinc oxide nanoparticles and bovine serum albumin. Journal of Biomolecular Structure & Dynamics, 38(4), 1248–1255. https://doi.org/10.1080/07391102.2019.1596838
   PubMed Web of Science ®Google Scholar
• Wang, X., Kong, X., Yu, Y., & Zhang, H. (2007). Synthesis and characterization of water-soluble and bifunctional ZnO − Au Nanocomposites. Journal Physical Chemistry, 111, 3836–3841.
   Web of Science ®Google Scholar
• Wen, M. G., Zhang, X. B., Tian, J. N., Ni, S. H., Bian, H. D., Huang, Y. L., & Liang, H. (2009). Binding interaction of xanthoxylin with bovine serum albumin. Journal of Solution Chemistry, 38(4), 391–401. https://doi.org/10.1007/s10953-009-9385-4
   Web of Science ®Google Scholar
• Wu, Y. L., Lim, C. S., Fu, S., Tok, A. I. Y., Lau, H. M., Boey, F. Y. C., & Zeng, X. T. (2007). Surface modifications of ZnO quantum dots for bio-imaging. Nanotechnology, 18(21), 215604. https://doi.org/10.1088/0957-4484/18/21/215604
   Web of Science ®Google Scholar
• Xiong, H. M., Xu, Y., Ren, Q. G., & Xia, Y. Y. (2008). Stable aqueous ZnO@polymer core-shell nanoparticles with tunable photoluminescence and their application in cell imaging. Journal of the American Chemical Society, 130(24), 7522–7523. https://doi.org/10.1021/ja800999u
   PubMed Web of Science ®Google Scholar
• Yewale, C., Baradia, D., Vhora, I., & Misra, A. (2013). Proteins: Emerging carrier for delivery of cancer therapeutics. Expert Opinion on Drug Delivery, 10(10), 1429–1448. https://doi.org/10.1517/17425247.2013.805200
   PubMed Web of Science ®Google Scholar
• Yu, X., Di, Y., Xie, C., Song, Y., He, H., Li, H., Pu, X., Lu, W., Fu, D., & Jin, C. (2015). An in vitro and in vivo study of gemcitabine-loaded albumin nanoparticles in a pancreatic cancer cell line. International Journal of Nanomedicine, 10, 6825–6834.
   PubMed Web of Science ®Google Scholar
• Zhou, Y., Wu, W., Hu, G., Wu, H., & Cui, S. (2008). Hydrothermal synthesis of ZnO nanorod arrays with the addition of polyethyleneimine. Materials Research Bulletin, 43(8-9), 2113–2118. https://doi.org/10.1016/j.materresbull.2007.09.024
   Web of Science ®Google Scholar
• Žūkienė, R., & Snitka, V. (2015). Zinc oxide nanoparticle and bovine serum albumin interaction and nanoparticles influence on cytotoxicity in vitro. Colloids and Surfaces. B, Biointerfaces, 135, 316–323. https://doi.org/10.1016/j.colsurfb.2015.07.054
   PubMed Web of Science ®Google Scholar