PLoS ONE 11(7):Įditor: Rajagopal Subramanyam, University of Hyderabad, INDIA (2016) A Comprehensive Spectroscopic and Computational Investigation to Probe the Interaction of Antineoplastic Drug Nordihydroguaiaretic Acid with Serum Albumins. 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.Ĭitation: Nusrat S, Siddiqi MK, Zaman M, Zaidi N, Ajmal MR, Alam P, et al. 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. 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. It also binds at site II of BSA but with lesser binding affinity (K b) ~10 5 M -1 and ΔG ~ -6.5 kcal.mol -1. #Half life blue shift loading dock freeNDGA binds to site II of HSA with binding constant (K b) ~10 5 M -1 and free energy (ΔG) ~ -7.5 kcal.mol -1. 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 & BSA) were examined by spectroscopic and computational methods. albumins, upon entering the circulatory system. 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.
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |