International E-publication: Publish Projects, Dissertation, Theses, Books, Souvenir, Conference Proceeding with ISBN.  International E-Bulletin: Information/News regarding: Academics and Research

Fluorescence Quenching Studies and Binding Interactions of β-Casein and Therapeutic Chemicals Mediated by Ag Nanoparticles and Cu Nanoparticles

Author Affiliations

  • 1 Department of Physical Chemistry, University of Madras, Guindy Campus, Chennai -600025, Tamilnadu,INDIA

Res.J.chem.sci., Volume 4, Issue (12), Pages 93-97, December,18 (2014)


Fluorescence quenching studies on the milk protein β Casein (BC) with certain chemotherapeutics acting as quenchers are studied. Around six organics such as urea (U), Thiourea(TU), Guanidine Hydrochloride (GHCl), 4-Amino antipyrine (AP), Paracetamol (P) and Guaiacol (G) are chosen as quenchers and found sensitive to addition of metal nanoparticles such as Silver nanoparticles (Ag nps) and Copper nanoparticles (Cu nps) respectively. The asynthesised Ag nps and Cu nps in this work possessed the mean sizes as 12±1nm and 18±1nm as found from HRTEM measurements. The extent of fluorescence quenching was found to be more in presence of metal nanoparticles than in absence of metal nanoparticles. The binding constant (K) and the number of binding sites (n) are obtained from Stern-Volmer plot and double reciprocal plot methods. The data indicate that the mediating capacity of Ag nps is higher than the Cu nps systems. This may be attributed to the smaller sized Ag nps than the Cu nps. The trend observed in the interaction between various organics and BC has been found to be U > TU > GHCl > AP > P > G. This trend remains the same even in the presence of metal nanoparticles. The exhibited interacting activity of the chemicals is attributed to the difference in the interaction of surfacial hydrophilic groups in BC with organics studied here.


  1. Chris H.J. Evers, Thorbjrn Andersson, Mikael Lund and Marie Skep, Langmuir, 28 (32), 1184311849 (2012)
  2. Bell.SJ, Grochoski. GT and Clarke AJ., Diabetes Metab Res Rev., Jan-Feb; 17(1), 51-4 (2001)
  3. Monetini L, Cavallo MG, Stefanini L, Ferrazzoli F, Bizzarri C, Marietti G, Curro V, Cervoni M, and Pozzilli P; IMDIAB Group, Diabetes Metab Res Rev., 17(1), 51-4 (2001)
  4. Alina Shapira, Yehuda G. Assaraf and Yoav D., Livney,Nanotechnology, Biology and Medicine,, 119-126 (2010)
  5. Bijan K. Paul, Narayani Ghosh, and Saptarshi Mukherjee, Langmuir, 30, 5921-5929 (2014)
  6. Stefano P. Boulos, Tyler A. Davis, Jie An Yang, Samuel E. Lohse, Alaaldin M. Alkilany, Lisa A. Holland, and Catherine J., Murphyl, Langmuir, 29 (48), 1498414996 (2013)
  7. Liu Y and Guo R, J Colloid Interface Sci, 332(1), 265-9 (2009)
  8. P. Bourassa, Bariyanga J. and Tajmir-Riahi H.A., J. Phys. Chem. B, 117 (5), 12871295 (2013)
  9. Hamid Reza Ghorbani, Nano-silver Colloidal Solution Formation by a Simple and Green Method, Oriental Journal of Chemistry, 30(2), (2014)
  10. Khatoon U.T., Nageswara Rao G.V.S.and Mohan M.K., Advanced Nanomaterials and Emerging Engineering Technologies (ICANMEET), (2013)
  11. Patwari G., Bodo B.J., Singha R. and Kalita P.K., Res. J. Chem. Sci., 3(9), 45-50 (2013)
  12. Pandey Bhawana and Fulekar M.H, Res. J. chem. sci., 2(2), 90-96 (2012)
  13. Hassan Hashemipour, Maryam Ehtesham Zadeh, Rabee Pourakbari and Payman Rahimi, International Journal of the Physical Sciences Vol. 6(18), 4331-4336 (2011)
  14. L. Guo, Z.H. Wu, K. Ibrahim, T. Liu, Y. Tao, and X. Ju, The European Physical Journal D, , 591594 (1999)
  15. Mara Eugenia Hidalgo, Bibiana D. Riquelme, Estela M. Alvarez, Jorge R. Wagner and Patricia H. Risso, Instituto de Fsica Rosario (IFIR), CONICET-UNR, (2000)
  16. Alexander G. Volkov, Liquid Interfaces In Chemical, Biological and Pharmaceutical Applications,
  17. Kevin N.P, New Zealand Dairy Research Institute, Palmerston North Eur. J. Biochem., 58, 23-29 (1975)
  18. Lucie Trnkov, Iva Bouov, Vladimr Kubek, and Jaroslav Drata, Natural Science, 2(6), 563-570 (2010)
  19. Shruti R Saptarshi, Albert Duschl and Andreas L Lopata, Journal of Nanobiotechnology, 11(26), (2013)
  20. Dorothy B. Calhoun, Jane M. Vanderkooi, Gary R. Holtorn, and Walter S. Englander, PROTEINS: Structure, Function, and Genetics, 1, 109-115(1986)
  21. Dulkeith.E, Morteani. A.C, Niedereichholz. T, Klar. T.A, and Feldmann. J, Physical Review Letters, 89(20), (2002)
  22. Stevenson. S.G and Preston. K.R, Surface Properties of Gluten Investigated by a Fluorescence Approach, Cereal Chem.71(2), 155-159 (1994)
  23. Suresh Kumar H.M., Kunabenchi R.S., Biradar J.S., Math N.N., Kadadevarmath J.S. and Inamdar S.R., Journal of Luminescence, 116(12), 3542 (2006)
  24. Mingxiong Tan, Weijiang Liang,Xujian Luo, and Yunqiong Gu, Journal of Chemistry, Article ID 308054 (2013)
  25. Yue Teng, Rutao Liu, Shifeng Yan, Xingren Pan, Pengjun Zhang, and Meijie Wang, J Fluoresc, 20, 381-387 (2010)
  26. Athina Papadopoulou, Rebecca J. Green, and Richard A. Frazier, J. Agric. Food Chem.(53), 158-163 (2005)
  27. V.N. Pustovit and T. V. Shahbazyan, J. Chem. Phys.(136), 204701 (2012)
  28. Abdelaziz Elalaoui', Gilles Divita', Georges Maury', Jean-Louis Imbach' and Roger S. Goody, Eur. J. Biochem.,(221), 839-846 (1994)