tetano
Editor, Senior Moderator
J Photochem Photobiol B. 2012 Nov 29;119C:65-70. doi: 10.1016/j.jphotobiol.2012.11.003. [Epub ahead of print]
A comparative study of the interaction of Tamiflu and Oseltamivir carboxylate with bovine serum albumin.
Vishkaee TS, Mohajerani N, Nafisi S.
Source
Department of Chemistry, Islamic Azad University, Central Tehran Branch (IAUCTB), Tehran, Iran.
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.
Copyright ? 2012 Elsevier B.V. All rights reserved.
PMID:
23353784
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23353784
A comparative study of the interaction of Tamiflu and Oseltamivir carboxylate with bovine serum albumin.
Vishkaee TS, Mohajerani N, Nafisi S.
Source
Department of Chemistry, Islamic Azad University, Central Tehran Branch (IAUCTB), Tehran, Iran.
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.
Copyright ? 2012 Elsevier B.V. All rights reserved.
PMID:
23353784
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23353784