Combined spectroscopic and molecular docking study of binding interaction of pyrano [3, 2-f] quinoli

Combined Spectroscopic And Molecular Docking Study Of Binding Interaction Of Pyrano [3, 2-f] Quinoline Derivatives With Bovine Serum Albumins And Its Application In Mammalian Cell Imaging

Swarup Roy1, Sudipta ponra2, Tapas Ghosh2, Ratan Sadhukhan1, K. C. Majumdar2*, Tapan Kumar Das1*

1Department of Biochemistry and Biophysics, University of Kalyani, Kalyani 741235, West Bengal, India

2Departments of Chemistry, University of Kalyani, Kalyani 741235, West Bengal, India

Adv. Mater. Lett., 2015, 6 (11), pp 1004-1011

DOI: 10.5185/amlett.2015.5941

Publication Date (Web): Oct 26, 2015



The interaction between pyrano [3, 2-f] quinoline derivatives (TPQ) and bovine serum albumin (BSA) was studied using spectroscopic techniques. The TPQ quench the fluorescence of BSA through dynamic quenching. According to Van’t Hoff equation, the thermodynamic parameters were calculated and which indicated hydrogen bonds and van der waals forces played a prime role in stabilizing the BSA–TPQ complexes. Also, the average binding distance (r) and the critical energy transfer distance (Ro) between TPQ and BSA were also evaluated according to Förster’s non-radiative energy transfer (FRET) theory. What is more, UV-visible and circular dichroism results showed that the addition of TPQ changed the secondary structure of BSA and led to a reduction in content α-helix (%) content. It was also observed that TPQ shows cell staining property to the cultured HeLa cell line. Theoretical docking study of interaction between BSA and TPQ also supported the experimental results. All the results suggested that BSA experienced substantial conformational changes induced by TPQ; this may be useful to study synthetic organic molecules for their application as pharmaceuticals.


Bovine serum albumin, TPQ, docking, spectroscopic method, cell staining.

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