Skip to main content Accessibility help
×
Home

Anti-Tumor Chloroquine-Gold Nanocomposites and their Binding Interaction with Bovine Serum Albumin: Biophysical and Biochemical Aspects of Protein Binding

  • Prachi Joshi (a1) (a2), Soumyananda Chakraborti (a3), Jaime E. Ramirez-Vick (a4), Z. A. Ansari (a2), Virendra Shanker (a1), Pinak Chakrabarti (a3) and Surinder P. Singh (a1) (a4)...

Abstract

We have conjugated chloroquine onto nano-sized, thiol-stabilized gold nanoparticles by using 1-ethyl-3-[3-dimethylaminopropyl] carbodiimide hydrochloride (EDC) / N-hydroxysulfosuccinimide (NHS) chemistry. The formation of gold nanoparticles was confirmed using optical spectra for characteristic surface plasmon band; the average size of gold nanoparticles was found to be 5-7 nm from electron microscopy measurements. The anti-tumor activity of prepared nanocomposite, vis-à-vis chloroquine itself, had been demonstrated using MCF-7 breast cancer cell line. To determine the binding affinity of gold-chloroquine nanocomposites to transport proteins present in blood serum, we studied the binding interaction of gold-chloroquine to bovine serum albumin (BSA), the most abundant plasma protein. The binding was studied by using isothermal titration calorimetry and fluorescence spectroscopy and was analyzed in terms of binding constant, entropy and enthalpy change. The gold-chloroquine nanocomposites were found to interact efficiently with BSA and fluorescence quenching experiments involving Trp212 suggests that the nanocomposites bind at site I of BSA.

Copyright

Corresponding author

*Address for correspondence: pinak@boseinst.ernet.in; surinder.singh@upr.edu

Footnotes

Hide All
$

Both the authors have equal contribution.

Footnotes

References

Hide All
1. Gao, J., Gu, H. and Xu, B., Acc. Chem. Res. 42, 10971107 (2009).
2. Dixit, V., Van den Bossche, J., Sherman, D.M., Thompson, D.H. and Andres, R.P., Bioconjugate Chem. 17, 603609 (2006).
3. You, C.C., Verma, A. and Rotello, V.M., Soft Matter 2, 190204 (2006).
4. Martinson, J.A., Montoya, C.J., Usuga, X., Ronquillo, R., Landay, A.L. and Desai, S.N., Antimicrob. Agents Ch. 54, 871(2010).
5. Navarro, M., Hernandez, C., Vasquez, F., Goitia, H., Ojeda, L.E., Velasquez, M. and Fraile, G., Transition Met. Chem. 33, 893898 (2008).
6. Martirosyan, A.R., Rahim-Bata, R., Freeman, A.B., Clarke, C.D., Howard, R.L. and Strobl, J.S., Biochem. Pharmacol. 68, 17291738 (2004).
7. Maclean, K.H., Dorsey, F.C., Cleveland, J.L. and Kastan, M.B., J. Clin. Invest. 118, 7988 (2008).
8. Jisha, V.S., Arun, K.T., Hariharan, M. and Ramaiah, D., J. Am. Chem. Soc. 128, 60246025 (2006).
9. Peters, T. Jr., Adv. Protein Chem. 37, 6006560065 (1985).
10. He, X.M. and Carter, D.C., Nature 358, 209215 (1992).
11. Lakowicz, J.R., Principles of Fluorescence Spectroscopy. 3rd ed.: Springer: New York, 2006.
12. Ware, W.R., J. Phys. Chem. 66, 455458 (1962).
13. Ross, P.D. and Subramanian, S., Biochemistry 20, 30963102 (1981).

Keywords

Anti-Tumor Chloroquine-Gold Nanocomposites and their Binding Interaction with Bovine Serum Albumin: Biophysical and Biochemical Aspects of Protein Binding

  • Prachi Joshi (a1) (a2), Soumyananda Chakraborti (a3), Jaime E. Ramirez-Vick (a4), Z. A. Ansari (a2), Virendra Shanker (a1), Pinak Chakrabarti (a3) and Surinder P. Singh (a1) (a4)...

Metrics

Full text views

Total number of HTML views: 0
Total number of PDF views: 0 *
Loading metrics...

Abstract views

Total abstract views: 0 *
Loading metrics...

* Views captured on Cambridge Core between <date>. This data will be updated every 24 hours.

Usage data cannot currently be displayed