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• W2004804710 endingPage "70" @default.
• W2004804710 startingPage "65" @default.
• W2004804710 abstract "Oseltamivir phosphate (Tamiflu) is a pro-drug that is metabolized to its active form (Oseltamivir carboxylate), after oral administration. OC inhibits influenza A and B neuraminidases in vitro and OP inhibits influenza virus infection and replication in vitro. Serum albumin is the most abundant of the proteins in the circulatory system of a wide variety of organisms and plays an important role in the transport and deposition of many drugs. The aim of this study was to examine the interaction of BSA with Tamiflu and Oseltamivir carboxylate in aqueous solution at physiological conditions, using a constant protein concentration and various drug contents. FTIR, UV-Vis spectroscopic methods were used to determine the drugs binding mode, the binding constant and the effects of drug complexation on protein secondary structure. Structural analysis showed that OP and OC bind BSA with overall binding constants of K(OP-BSA)=1.88 (±0.16)×10(4)M(-1) and K(OC-BSA)=5.7 (±0.09)×10(2)M(-1). Drug complexation alters protein conformation by major reduction of α-helix and random coil and increase of β-sheet and turn structures that indicate a partial protein destabilization. The results suggest that BSA might act as carrier proteins for OP in delivering it to target molecules." @default.
• W2004804710 created "2016-06-24" @default.
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• W2004804710 creator A5036144872 @default.
• W2004804710 creator A5084088435 @default.
• W2004804710 date "2013-02-01" @default.
• W2004804710 modified "2023-10-14" @default.
• W2004804710 title "A comparative study of the interaction of Tamiflu and Oseltamivir carboxylate with bovine serum albumin" @default.
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• W2004804710 doi "https://doi.org/10.1016/j.jphotobiol.2012.11.003" @default.
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• W2004804710 hasPublicationYear "2013" @default.
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