Complexation Peculiarities in “Doxorubicin–Bovine Serum Albumin–Gold Nanoparticles” Heterosystem. The Fluo-rescence Study

  • N. A. Goncharenko Taras Shevchenko National University of Kyiv, Faculty of Physics
  • O. P. Dmytrenko Taras Shevchenko National University of Kyiv, Faculty of Physics
  • O. L. Pavlenko Taras Shevchenko National University of Kyiv, Faculty of Physics
  • M. P. Kulish Taras Shevchenko National University of Kyiv, Faculty of Physics
  • I. P. Pundyk Taras Shevchenko National University of Kyiv, Faculty of Physics
  • A. I. Lesyuk Taras Shevchenko National University of Kyiv, Faculty of Physics
  • T. O. Busko Taras Shevchenko National University of Kyiv, Faculty of Physics
  • A. M. Lopatynskyy V.E. Lashkaryov Institute of Semiconductor Physics, Nat. Acad. of Sci. of Ukraine
  • V. I. Chegel V.E. Lashkaryov Institute of Semiconductor Physics, Nat. Acad. of Sci. of Ukraine
  • V. K. Lytvyn V.E. Lashkaryov Institute of Semiconductor Physics, Nat. Acad. of Sci. of Ukraine
  • M. I. Kaniuk O.V. Palladin Institute of Biochemistry, Nat. Acad. of Sci. of Ukraine
Keywords: doxorubicin, bovine serum albumin, gold nanoparticles, complexation, fluorescence, localized surface plasmon resonance


The fluorescence (FL) quenching in aqueous solutions of doxorubicin (DOX)–bovine serum albumin (BSA)–gold nanoparticles (AuNPs) is studied. The existence of additional mechanisms of DOX-BSA complex formation leading to an increase in the binding constant K and a decrease in the number of binding sites n and the distance between the fluorophore and energy acceptors due to the presence of gold nanoparticles is shown.


F. Arcamone. Doxorubicin, Anticancer Antibiotics (Academic Press, 1981) [ISBN: 9780323139731].

K. Krohn. Book review: Anthracycline antibiotics Angew. Chemie 95, 649 (1983).

A. Garnier-Suillerot, C. Marbeuf-Gueye, M. Salerno et al. Analysis of drug transport kinetics in multidrug-resistant cells: Implications for drug action. Curr. Med. Chem. 8, 51 (2001).

C. Monneret. Recent developments in the field of antitumour anthracyclines. Eur. J. Med. Chem. 36, 483 (2001).

M.N. Preobrazhenskaya, A.N. Tevyashova, E.N. Olsufyeva et al. Second generation drugs-derivatives of natural antitumor anthracycline antibiotics daunorubicin. J. Med. Sci. 26, 119 (2006).

A.N. Tevyashova. Development of progrugs on the basis of anthracycline antibiotics. Vestn. MITKhT 9, 11 (2014).

M.P. Evstigneev, A.S. Buchelnikov, D.P. Voronin et al. Complexation of C60 fullerene with aromatic drugs. Chem. Phys. Chem. 14, 568 (2013).

Y.I. Prylutskyy, M.P. Evstigneev, I.S. Pashkova et al. Characterization of C60 fullerene complexation with antibiotic doxorubicin. Phys. Chem. Chem. Phys. 16, 23164 (2014).

Y.I. Prylutskyy, M.P. Evstigneev, V.V. Cherepanov et al. Structural organization of C60 fullerene, doxorubicin, and their complex in physiological solution as promising antitumor agents. J. Nanoparticle Res. 17, 45 (2015).

R.R. Panchuk, S.V. Prylutska, V.V. Chumak et al. Application of C60 fullerene-doxorubicin complex for tumor cell treatment in vitro and in vivo. J. Biomed. Nanotechnol. 11, 1139 (2015).

Y.I. Prylutskyy, V.V. Cherepanov, M.P. Evstigneev et al. Structural self-organization of C60 and cisplatin in physiological solution. Phys. Chem. Chem. Phys. 17, 26084 (2015).

A.A. Mosunov, I.S. Pashkova, M. Sidorova et al. Determination of the equilibrium constant of C60 fullerene binding with drug molecules. Phys. Chem. Chem. Phys. 19, 6777 (2017).

Y. Prylutskyy, A. Borowik, G. Golunski et al. Biophysical characterization of the complexation of C60 fullerene with doxorubicin in a prokaryotic model. Materwiss. Werksttech. 47, 92 (2016).

Y.I. Prylutskyy, V.V. Cherepanov, V.V. Kostjukov et al. Study of the complexation between Landomycin A and C60 fullerene in aqueous solution. RSC Adv. 6, 81231 (2016).

S. Prylutska, R. Panchuk, G. Golunski et al. C60 fullerene enhances cisplatin anticancer activity and overcomes tumor cell drug resistance. Nano Res. 10, 652 (2017).

B. X. Li. Nano-oncology. Harvard Sci. Rev. Small Sci. 19, 42 (2006).

S. Nie, Y. Xing, G. J. Kim et al. Nanotechnology applications in cancer. Annu. Rev. Biomed. Eng. 9, 257 (2007).

L. Prinzen, R.-J.J.H.M. Miserus, A. Dirksen et al. Optical and magnetic resonance imaging of cell death and platelet activation using annexin A5-functionalized quantum dots. Nano Lett. 7, 93 (2007).

I.V. Plyuto, A.P. Shpak, A.A. Zaporozhets et al. Nanomaterials and Nanocomposites in Medicine, Biology, and Ecology (Naukova Dumka, 2011) (in Russian).

V. Orel, A. Romanov, O. Rykhalskyi et al. Antitumor effect of superparamagnetic iron oxide nanoparticles conjugated with doxorubicin during magnetic nanotherapy of Lewis Lung carcinoma. Materwiss. Werksttech. 47, 165 (2016).

V.V. Turov, Y.I. Prylutskyy, T.V. Krupskaya et al. Clustering of hydrochloric acid on the surface of C60/C70 fullerite and its composites with nanosilica. Materwiss. Werksttech. 47, 172 (2016).

T. Zhu, X. Fu, T. Mu et al. pH-dependent adsorption of gold nanoparticles on p-aminothiophenol-modified gold substrates. Langmuir 15, 5197 (1999).

D.P. O'Neal, L.R. Hirsch, N.J. Halas et al. Photo-thermal tumor ablation in mice using near infrared-absorbing nanoparticles.Cancer Lett. 209, 171 (2004).

P.K. Jain, I.H. El-Sayed, M.A. El-Sayed. Au nanoparticles target cancer. Nano Today 2, 18 (2007).

X. Liu, M. Atwater, J. Wang et al. Extinction coefficient of gold nanoparticles with different sizes and different capping ligands. Colloids Surfaces B Biointerfaces 58, 3 (2007).

A.M. Lopatynskyi, O.G. Lopatynska, V.I. Chegel et al. Localized surface plasmon resonance biosensor-part I: Theoretical study of sensitivity-extended Mie approach. IEEE Sens. J. 11, 361 (2011).

S. Zeng, K.-T. Yong, I. Roy et al. A review on functionalized gold nanoparticles for biosensing applications. Plasmonics 6, 491 (2011).

A.M. Goodman, Y. Cao, C. Urban et al. The surprising in vivo instability of near-IR-absorbing hollow Au-Ag nanoshells. ACS Nano 8, 3222 (2014).

A.J. Trouiller, S. Hebie, F. El Bahhaj et al. Chemistry for oncotheranostic gold nanoparticles. Eur. J. Med. Chem. 99, 92 (2015).

J. Zhu, W. Li, M. Zhu et al. Influence of the pH value of a colloidal gold solution on the absorption spectra of an LSPR-assisted sensor. AIP Adv. 4, 1 (2014).

M. Xiao, Y.M. Chen, M.N. Biao et al. Bio-functionalization of biomedical metals. Mater. Sci. Eng. C 70, 1057 (2017).

Yu.P. Meshalkin, N.P. Bgatova. Perspectives and problems of the application of inorganic nanoparticles to oncologggy. J. Sib. Fed. Univ. Biol. 3, 248 (2008).

N.A. Goncharenko, O.L. Pavlenko, O.P. Dmytrenko et al. Gold nanoparticles as a factor of influence on doxorubicin-bovine serum albumin complex. Appl. Nanosci. 9, 825 (2019).

K. Vuignier, J. Schappler, J.-L. Veuthey et al. Drug-protein binding: A critical review of analytical tools. Anal. Bioanal. Chem. 398, 53 (2010).

J. Pan, Z. Ye, X. Cai et al. Biophysical study on the interaction of ceftriaxone sodium with bovine serum albumin using spectroscopic methods. J.Biochem. Mol. Toxicol. 26, 487 (2012).

Q. Yue, T. Shen, C.Wang et al. Study on the interaction of bovine serum albumin with ceftriaxone and the inhibition effect of zinc (II). Int. J. Spectrosc. 1 (2012).

J.Wu, R.Wei, H.Wang et al. Underlying the mechanism of vancomycin and human serum albumin interaction: A biophysical study. J. Biochem. Mol. Toxicol. 27, n/a (2013).

A. Sulkowska. Interaction of drugs with bovine and human serum albumin. J. Mol. Struct. 614, 227 (2002).

A. Mallick, S. Maiti, B. Haldar et al. Photophysics of 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine: Emission from two states. Chem. Phys. Lett. 371, 688 (2003).

L. Birla, A. M. Cristian, M. Hillebrand. Absorption and steady state fluorescence study of interaction between eosin and bovine serum albumin. Spectrochim. Acta - Part A Mol. Biomol. Spectrosc. 60, 551 (2004).

L. Trynda-Lemiesz. Paclitaxel-HSA interaction. Binding sites on HSA molecule. Bioorganic Med. Chem. 12, 3269 (2004).

S. Deepa, A.K. Mishra. Fluorescence spectroscopic study of serum albumin-bromadiolone interaction: Fluorimetric determination of bromadiolone. J. Pharm. Biomed. Anal. 38, 556 (2005).

S. Bi, Y. Sun, C. Qiao et al. Binding of several anti-tumor drugs to bovine serum albumin: Fluorescence study. J. Lumin. 129, 541 (2009).

D. Agudelo, P. Bourassa, J. Bruneau et al. Probing the binding sites of antibiotic drugs doxorubicin and N-(trifluoroacetyl) doxorubicin with human and bovine serum albumins. PLoS One 7, 1 (2012).

How to Cite
Goncharenko, N., Dmytrenko, O., Pavlenko, O., Kulish, M., Pundyk, I., Lesyuk, A., Busko, T., Lopatynskyy, A., Chegel, V., Lytvyn, V., & Kaniuk, M. (2020). Complexation Peculiarities in “Doxorubicin–Bovine Serum Albumin–Gold Nanoparticles” Heterosystem. The Fluo-rescence Study. Ukrainian Journal of Physics, 65(6), 468.
Optics, atoms and molecules