[Bacterial overexpression of the human interleukin-2 in insoluble form via the pET Trx fusion system]

Selection of a system for successful recombinant protein production is important. The aim of this study was to produce high levels of human interleukin-2 [hIL-2] in soluble form. To this end, the pET32a vector in Escherichia coli BL21 [DE3] was used as an expression system, since it was previously used for the production of mouse IL-2 in soluble form. The results indicated that contrary to expectations, the expressed protein was in the form of inclusion bodies and perhaps amino acid differences between human and mouse IL-2 should be determinant. The hIL-2 protein is a small peptide, therefore its recovery as a biologically functional protein by the process of refolding may be feasible and could lead to high yields at the industrial scale

effects of acetaminophen on human serum albumin [HSA]

Thermal conformational changes in human serum albumin [HSA] in present with a 10 mM phosphate buffer, at pH=7 have been investigated via circular dichroism [CD] and UV spectroscopic methods. The results indicate that temperature in a range of 25oC to 55oC could induce a reversible conformational change in the structure of HSA. The HSA phase transition corresponds to the physiological and pathological conditions of the body, especially fever. The conformational change observed in HSA is accompanied by a mild conversion of its secondary structures. Acetaminophen is a papular pain killer, and HSA is used as a drug carrier. Hence, acetaminophen could it interact with HSA. The study of HSA - acetaminophen interaction reveals the effects of acetaminophen on HSA structure, preventing it's phase transition. HSA - acetaminophen interaction leads to the stabilization of HAS. This interaction is accompanied with 8 kJ/mol of free energy change. The structural changes within HSA due to it's interaction with acetaminophen could be considered as a drug side effect and it may affect the protein functions