Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5399334 | Journal of Luminescence | 2015 | 8 Pages |
Abstract
Interaction of pharmacologically important anticancer drug cytosine β-D arabinofuranoside with human serum albumin (HSA) at physiological pH 7.4 has been studied by utilizing various spectroscopic and molecular docking strategies. Fluorescence results revealed that cytosine β-D arabinofuranoside interacts with HSA through static quenching mechanism with binding affinity of 2.4Ã103 Mâ1. The average binding distance between drug and Trp214 of HSA was found to be 2.23 nm on the basis of the theory of Förster's energy transfer. Synchronous fluorescence data indicated that interaction of drug with HSA changed the microenvironment around the tryptophan residue. UV-visible spectroscopy and circular dichroism results deciphered the complex formation and conformational alterations in the HSA respectively. Dynamic light scattering was utilized to understand the topology of protein in absence and presence of drug. Thermodynamic parameters obtained from isothermal titration calorimetry (ÎH=â26.01 kJ molâ1 and TÎS=6.5 kJ molâ1) suggested the involvement of van der Waal interaction and hydrogen bonding. Molecular docking and displacement study with site specific markers suggested that cytosine β-D arabinofuranoside binds to subdomain IB of HSA which is also known as the hemin binding site. This study will be helpful to understand the binding mechanism of cytosine β-D arabinofuranoside with HSA and associated alterations.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Parvez Alam, Sumit Kumar Chaturvedi, Tamanna Anwar, Mohammad Khursheed Siddiqi, Mohd Rehan Ajmal, Gamal Badr, Mohamed H. Mahmoud, Rizwan Hasan Khan,