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
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E-mail: tapankumardas175@gmail.com, kcmklyuniv@gmail.com
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.
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