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The intermolecular interaction of prednisolone with bovine serum albumin (BSA) was studied using fluorescence, circular dichroism (CD) and molecular docking methods. The experimental results showed that the fluorescence quenching of the BSA at 338 nm by prednisolone resulted from the formation of prednisolone-BSA complex. The number of binding sites (n) for prednisolone binding on BSA was approximately equal to 1. Base on the sign and magnitude of the enthalpy and entropy changes (ΔH(0)=-149.6 kJ mol(-1) and ΔS(0)=-370.7 J mol(-1)K(-1)) and the results of molecular docking, it could be suggested that the interaction forces were mainly Van der Waals and hydrogen bonding interactions. Moreover, in the binding process of BSA with prednisolone, prednisolone molecule can be inserted into the hydrophobic cavity of subdomain IIIA (site II) of BSA. The distance between prednisolone and Trp residue of BSA was calculated as 2.264 nm according to Forster's non-radiative energy transfer theory. Copyright © 2012 Elsevier B.V. All rights reserved.


Jie-hua Shi, Ying-Yao Zhu, Jing Wang, Jun Chen, Ya-Jing Shen. Intermolecular interaction of prednisolone with bovine serum albumin: spectroscopic and molecular docking methods. Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy. 2013 Feb 15;103:287-94

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PMID: 23261625

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