A Comprehensive Spectroscopic and Computational Investigation to Probe the Interaction of Antineoplastic Drug Nordihydroguaiaretic Acid with Serum AlbuminsReport as inadecuate




A Comprehensive Spectroscopic and Computational Investigation to Probe the Interaction of Antineoplastic Drug Nordihydroguaiaretic Acid with Serum Albumins - Download this document for free, or read online. Document in PDF available to download.

Exogenous drugs that are used as antidote against chemotheray, inflammation or viral infection, gets absorbed and interacts reversibly to the major serum transport protein i.e. albumins, upon entering the circulatory system. To have a structural guideline in the rational drug designing and in the synthesis of drugs with greater efficacy, the binding mechanism of an antineoplastic and anti-inflammatory drug Nordihydroguaiaretic acid NDGA with human and bovine serum albumins HSA and BSA were examined by spectroscopic and computational methods. NDGA binds to site II of HSA with binding constant Kb ~105 M-1 and free energy ΔG ~ -7.5 kcal.mol-1. It also binds at site II of BSA but with lesser binding affinity Kb ~105 M-1 and ΔG ~ -6.5 kcal.mol-1. The negative value of ΔG, ΔH and ΔS for both the albumins at three different temperatures confirmed that the complex formation process between albumins and NDGA is spontaneous and exothermic. Furthermore, hydrogen bonds and hydrophobic interactions are the main forces involved in complex formation of NDGA with both the albumins as evaluated from fluorescence and molecular docking results. Binding of NDGA to both the albumins alter the conformation and causes minor change in the secondary structure of proteins as indicated by the CD spectra.



Author: Saima Nusrat, Mohammad Khursheed Siddiqi, Masihuz Zaman, Nida Zaidi, Mohammad Rehan Ajmal, Parvez Alam, Atiyatul Qadeer, Ali Sabe

Source: http://plos.srce.hr/



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