Jump to main content
Jump to site search


A comprehensive spectroscopic and computational investigation on the binding of anti-asthmatic drug triamcinolone with serum albumin

Abstract

The biomolecular interaction of triamcinolone with bovine serum albumin (BSA) was performed using various multi-spectroscopic techniques in combination with in silico studies. UV-visible absorption, fluorescence spectroscopy and resonance Rayleigh scattering studies confirmed the formation of BSA- triamcinolone complex. The binding constant was found to be in the order of 103 M-1. Conformational and microenvironmental changes in BSA after addition of triamcinolone were confirmed by circular dichroism and 3D fluorescence spectroscopy, respectively. The negative values of ΔG and ΔH confirmed spontaneous and exothermic binding. The average binding distance between BSA and triamcinolone was also calculated through FRET. Additionally, the effect of metal ions and β-cyclodextrin on the binding of triamcinolone with BSA was also investigated. Molecular docking and site marker displacement experiments unveiled the binding of triamcinolone to BSA at site III located in subdomain IB of BSA. Molecular dynamics simulation showed lower RMSD value and negative total energy suggesting favourable binding between BSA and triamcinolone.

Back to tab navigation

Publication details

The article was received on 01 Nov 2018, accepted on 01 Feb 2019 and first published on 05 Feb 2019


Article type: Paper
DOI: 10.1039/C8NJ05486J
Citation: New J. Chem., 2019, Accepted Manuscript

  •   Request permissions

    A comprehensive spectroscopic and computational investigation on the binding of anti-asthmatic drug triamcinolone with serum albumin

    M. Tabish, S. Siddiqui, F. Ameen, I. Jahan and S. M. Nayeem, New J. Chem., 2019, Accepted Manuscript , DOI: 10.1039/C8NJ05486J

Search articles by author

Spotlight

Advertisements