Swarup Roy; Sudipta ponra; Tapas Ghosh; Ratan Sadhukhan; K. C. Majumdar; Tapan Kumar Das
Abstract
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 ...
Read More
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.
Swarup Roy; Sudipta Ponra; Raj Kumar Nandi; K. C. Majumdar; Tapan Kumar Das
Abstract
The study of interaction between spirooxindole-annulated thiopyran derivatives (STP) and bovine serum albumin (BSA) was investigated using multi-spectroscopic and docking method. The intrinsic fluorescence of BSA could effectively quenched by STP through dynamic quenching. The thermodynamic parameters ...
Read More
The study of interaction between spirooxindole-annulated thiopyran derivatives (STP) and bovine serum albumin (BSA) was investigated using multi-spectroscopic and docking method. The intrinsic fluorescence of BSA could effectively quenched by STP through dynamic quenching. The thermodynamic parameters suggested that hydrogen bonds and van der Waals forces played a key role in stabilizing the BSA–STP complexes. According to Forster non radiation energy transfer theory (FRET) the average binding distance (r) between STP and BSA were found to be < 7 nm. Furthermore, UV-visible and circular dichroism results indicated that in presence of STP secondary structure of BSA changed. Theoretical docking study of the interaction of BSA and STP also supported the experimental results.