NDLI: Comparative binding study of anti-tuberculosis drug pyrazinamide with serum albumins

Content Provider	Royal Society of Chemistry (RSC)
Author	Zaman, Masihuz Chaturvedi, Sumit Kumar Siddiqi, Mohammad Khursheed Khan, Rizwan Hasan Alam, Parvez
Copyright Year	2016
Abstract	The interaction of anti-tuberculosis drug pyrazinamide (PYZ) with serum albumins (HSA and BSA) has been studied using spectroscopic and molecular docking approaches. The effects of PYZ on the protein conformation, topology and stability were determined using Circular Dichroism (CD), Dynamic Light Scattering (DLS) and Differential Scanning Calorimetry (DSC). The obtained binding constant (Kb) was ∼104 M−1 for both HSA and BSA, although a higher affinity of PYZ was found with BSA. A higher value for the Gibbs free energy reflects that PYZ interacts more favourably with BSA. A reduction in the hydrodynamic radii and increase in the secondary structural content of the protein confirm that the serum albumins stabilize on binding with PYZ. Furthermore, elevation of the transition melting point also supports the stabilizing action of PYZ. Furthermore, site specific markers and a molecular docking study confirmed the binding location of PYZ with HSA and BSA. The present study will be helpful for understanding the binding of PYZ and associated alterations in the stability and conformation of serum albumins.
Starting Page	85860
Ending Page	85869
Page Count	10
File Format	HTM / HTML PDF
ISSN	20462069
Volume Number	6
Issue Number	89
Journal	RSC Advances
DOI	10.1039/c6ra10487h
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Gibbs free energy Hydrodynamic radius Docking (molecular) Binding constant Gibbs Topology Pyrazinamide Protein Circular dichroism BSA Dynamic light scattering HSA Calorimetry Protein structure
Content Type	Text
Resource Type	Article
Subject	Chemistry Chemical Engineering

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