• Suja Abraham Department of Physics, Hindustan Institute of Technology and Science, India
  • Vellaichamy Parthasarathy Department of Physics, Hindustan Institute of Technology and Science, India



Protein, Copper oxide nanoparticles, Spectroscopy, Structural changes


Objective: Since structural changes of adsorbed protein are necessary for cellular uptake of nanoparticles (NPs) it is of prime importance to know about structural changes of bovine serum albumin (BSA) when it interacts with CuO NPs–a potential new antitumor drug.

Methods: CuO NPs prepared by sol-gel technique were characterized by x-ray diffraction (XRD) and tunneling electron microscope (TEM) techniques. The conformational changes induced by CuO NPs on BSA were studied by various spectroscopic techniques such as steady state and time-resolved fluorescence measurements. The changes in fluorescence emission parameters such as fluorescence intensity, fluorescence emission maximum and lifetimes of fluorescent residues in BSA were studied.

Results: XRD analysis showed the average particle size as 32 nm. The TEM micrograph showed particles of different size varying from 10 to 45 nm. Fluorescence quenching was confirmed due to a decrease in fluorescence intensity of CuO NPs–BSA complex. The analysis of lifetime measurements indicated BSA contained two tryptophan (trp) residues that fluoresced in different environments. Static quenching mechanism was confirmed by time-resolved measurements when BSA interacted with CuO NPs.

Conclusion: Minor structural changes of BSA protein were observed during the interaction studies.


Download data is not yet available.


Seigneuric R, Markey L, Nuyten DSA, Dubernet C, Evelo CTA, Finot E, Garrido C. From nanotechnology to nanomedicine: applications to cancer research. Curr Mol Med 2010;10:640–52.

Renu K. Nanoparticles: a promising drug delivery approach. Asian J Pharm Clin Res 2018;11:30-5.

Jessy S, Ipshita M. Recent advances in nanocarrier based therapeutic and diagnostic tools for colorectal cancer. Int J Curr Pharm Res 2015;7:9-16.

Jyotibala B. Application of nanotechnology in food technology and targeted drug therapy for prevention of obesity: an overview. J Crit Rev 2017;4:7-11.

Swati JS, Praseetha PK, Sakthivel G. Targetted therapy for breast cancer cells by herbal drug formulations of iron oxide nanoparticles. Asian J Pharm Clin Res 2016;9:347-53.

Hajra KM, Liu JR. Apoptosome dysfunction in human cancer. Apoptosis 2004;6:691–704.

Vinardell MP, Mitjans M. Antitumor activities of metal oxide nanoparticles. Nanomaterials 2015;5:1004-21.

Wang Y, Zi XY, Su J, Zhang HX, Zhang XR, Zhu HY, et al. Cuprous oxide nanoparticles selectively induce apoptosis of tumor cells. Int J Nanomed 2012;7:2641–52.

Manyasree D, Kiran MP, Ravikumar R. CuO nanoparticles: synthesis, characterization and their bactericidal efficacy. Int J Appl Pharm 2017;9:71-4.

Olson RE, Christ DD. Plasma protein binding of drugs. Annu Rep Med Chem 1996;31:327–36.

Jung Se H, Choi SJ, Kim HJ. Molecular characteristics of bovine serum albumin-dextran conjugates. Biosci Biotechnol Biochem 2006;70:2064–70.

Lakowicz JR. Principles of fluorescence spectroscopy. 2nd edn. Dordrecht: Kluwer Academic Publishers; 1999.

Shang L, Wang YZ, Jiang JG. pH-dependent protein conformational changes in albumin: gold nanoparticle bioconjugates: a spectroscopic study. Langmuir 2007;23:2714–21.

Fleischer CC, Christine K Payne. The secondary structure of corona proteins determines the cell surface receptors used by nanoparticles. J Phys Chem B 2014;118:14017−26.

Tokonami S, Shiigi H, Nagaoka T. Preparation of nanogapped gold nanoparticle array for DNA detection. Electroanalysis 2008;20:355–60.

Kshirsagar M, Shrivastava R, Adwani S. Preparation and characterization of copper oxide nanoparticles and determination of enhancement in critical heat flux. Therm Sci 2017;21:1233-42.

Sun T, Liu L, Sun Y, Tan C, Yao F, Liang X, et al. Synthesis and characterization of TiO2 nanoparticles: applications in research on the interaction of colloidal TiO2 with Human serum albumin by fluorescence spectroscopy. Anal Sci 2012;28:491-6.

Lakowicz JR. Principles of fluorescence spectroscopy. 3rd edn. New York: Springer; 2008.

Bhunia AK, Samanta PK, Saha S, Kamilya T. ZnO nanoparticle-protein interaction: Corona formation with associated unfolding. Appl Phys Lett 2013;103:143701.

Kathiravan A, Renganathan R. Interaction of colloidal TiO2 with bovine serum albumin: a fluorescence quenching study. Colloids Surf A 2008;324:176–80.

Kathiravan A, Renganathan R, Anandan S. Interaction of colloidal AgTiO2 nanoparticles with bovine serum albumin. Polyhedron 2009;28:157–61.

Maity M, Pramanik SK, Pal U. Copper (I) oxide nanoparticle and tryptophan as its biological conjugate: a modulation of cytotoxic effects. J Nanopart Res 2014;16:2179.

Bhogale A, Patel N, Sarpotdar P, Mariam J, Dongre PM, Miotello A, et al. Systematic investigation on the interaction of bovine serum albumin with ZnO nanoparticles using fluorescence spectroscopy. Colloids Surf B 2013;102:257–64.

Bhogale A, Patel N, Mariam J. Comprehensive studies on the interaction of copper nanoparticles with bovine serum albumin using various spectroscopies. Colloids Surf B 2014;113:276–84.

Latheef SAA, Chakravarthy G, Mallaiah D. Spectroscopic and computational analysis of protein binding on copper nanoparticles: an insight into ligand and nanocarrier interaction. J Appl Spectrosc 2016;83:896-902.

Mariam J, Dongre PM, Kothari DC. Study of interaction of silver nanoparticles with bovine serum albumin using fluorescence spectroscopy. J Fluoresc 2011;21:2193–9.

Jhonsi MA, Kathiravan A, Renganathan R. Spectroscopic studies on the interaction of colloidal capped CdS nanoparticles with bovine serum albumin. Colloids Surf B 2009;72:167-72.

Rajeshwari A, Sunandan P, Swayamprava D, Madhumita V, Chandrasekaran N, Amitava M. Spectroscopic studies on the interaction of bovine serum albumin with Al2O3 nanoparticles. J Lumin 2014;145:859–65.

Kelkar DA, Chaudhuri A, Haldar S, Chattopadhyay A. Exploring tryptophan dynamics in acid-induced molten globule state of bovine alpha-lactalbumin: a wavelength-selective fluorescence approach. Eur Biophys J 2010;39:1453-63.

De Llanos R, Sanchez Cortes S, Domingo C. Surface plasmon effects on the binding of antitumoral drug emodin to bovine serum albumin. J Phys Chem C 2011;115:12419–29.

Johansson JS. Binding of the volatile anaesthetic chloroform to albumin demonstrated using tryptophan fluorescence quenching. J Biol Chem 1997;272:17961–5.

Togashi DM, Ryder AG, Mahon DM, Dunne P, McManus J. Fluorescence study of bovine serum albumin and Ti and Sn oxide nanoparticles Interactions. Proc SPIE-OSA Biomed Optics 2007;6628:1605-22.

Voicescu M, Ionescus S, Daniel GA. Spectroscopic and coarse-grained simulation studies of BSA and HSA protein adsorption on silver nanoparticles. J Nanopart Res 2012;14:1174.

Esfandfar P, Falahati M, Saboury AA. Spectroscopic studies of the interaction between CuO nanoparticles and bovine serum albumin. J Biomol Struct Dyn 2016;34:1962-8.

Kathiravan A, Paramaguru G, Renganathan R. Study on the binding of colloidal zinc oxide nanoparticles with bovine serum albumin. J Mol Struct 2009;934:129-34.

Gao XY, Wen W, Song ZY, Zhang AP, Hao J, Huang Q. Effects of rare earth ions on the interaction between nano TiO2 and bovine serum albumin in the presence of ultrasound. Acta Phys Chim Sin 2012;28:417-22.

Ojha K, Chowdhury PK, Ganguly AK. Fluorescence and CD studies of protein denaturation in the presence of sub picomolar gold nanoparticles. Indian J Chem 2012;51:1561-6.

Monopoli MP, Aberg C, Salvati A, Dawson KA. Biomolecular coronas provide the biological identity of nanosized materials. Nat Nano 2012;7:779-86.

Walkey CD, Chan WC. Understanding and controlling the interaction of nanomaterials with proteins in a physiological environment. Chem Soc Rev 2012;41:2780-99.

Garg A, Manidhar DM, Gokara M, Malleda C, Reddy CS. Elucidation of the binding mechanism of coumarin derivatives with human serum albumin. PLoS One 2013;8:e63805.

Soares S, Mateus N, De Freitas V. Interaction of different polyphenols with bovine serum albumin and human salivary α-amylase by fluorescence quenching. J Agric Food Chem 2007;55:6726–35.



How to Cite

Abraham, S., and V. Parthasarathy. “INTERACTION OF COPPER OXIDE NANOPARTICLES WITH BOVINE SERUM ALBUMIN BY SPECTROSCOPIC STUDIES”. International Journal of Pharmacy and Pharmaceutical Sciences, vol. 10, no. 5, May 2018, pp. 35-38, doi:10.22159/ijpps.2018v10i5.24877.



Original Article(s)