Recent progress in combinatorial drug has led to the generation of a large number of new compounds. microemulsions are versatile systems of great technological and scientific interest to the researchers because of their potential to incorporate a wide range of drug molecules (hydrophilic and hydrophobic) due to the presence of both lipophilic and hydrophilic domains.
Background: The efficacy and safety of 6-mercaptopurine (6-MP) therapy rely on the concentration of its metabolites. The aim of the current study is the pharmacokinetic analysis of 6-MP and the detection of its metabolites as well as the role of Thiopurine S-methyl transferase (TPMT), the enzyme associated with 6-MP metabolism, as a pharmacogenomics biomarker.
Heat shock protein 90 (Hsp90) is 90 kDa highly conserved dimeric chaperone protein in prokaryotic and eukaryotic cells and it is localized in different parts of the cell. Hsp90AA1 (inducible) and Hsp90AB1 (constitutive) are available in the cytosol; Grp94 and TRAP1 exist in endoplasmic reticulum and mitochondria; respectively. In unstressed cells, expression level of Hsp90 corresponds to 1-2% of total cellular protein, and Hsp90 is responsible for protein folding, maintenance and degradation of misfolded proteins, cell cycle control, and cellular signaling.
International Journal of Pharmaceutical Sciences and Developmental Research