Hostname: page-component-8448b6f56d-m8qmq Total loading time: 0 Render date: 2024-04-19T22:50:21.602Z Has data issue: false hasContentIssue false

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

Published online by Cambridge University Press:  21 March 2011

Prachi Joshi
Affiliation:
National Physical Laboratory, Dr. K. S. Krishnan Marg, New Delhi-110012, India. Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi-110025, India.
Soumyananda Chakraborti
Affiliation:
Department of Biochemistry, Bose Institute, P-1/12 CIT Scheme VIIM, Kolkata-700054, India.
Jaime E. Ramirez-Vick
Affiliation:
Engineering Science and Materials Department, University of Puerto Rico, Mayaguez, PR 00680, USA.
Z. A. Ansari
Affiliation:
Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi-110025, India.
Virendra Shanker
Affiliation:
National Physical Laboratory, Dr. K. S. Krishnan Marg, New Delhi-110012, India.
Pinak Chakrabarti*
Affiliation:
Department of Biochemistry, Bose Institute, P-1/12 CIT Scheme VIIM, Kolkata-700054, India.
Surinder P. Singh*
Affiliation:
National Physical Laboratory, Dr. K. S. Krishnan Marg, New Delhi-110012, India. Engineering Science and Materials Department, University of Puerto Rico, Mayaguez, PR 00680, USA.
*
*Address for correspondence: pinak@boseinst.ernet.in; surinder.singh@upr.edu
*Address for correspondence: pinak@boseinst.ernet.in; surinder.singh@upr.edu
Get access

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.

Type
Research Article
Copyright
Copyright © Materials Research Society 2011

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

Footnotes

$

Both the authors have equal contribution.

References

REFERENCES

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