Acetaminophen effects on human serum albumin (HSA)

Thermal conformational changes in human serum albumin (HSA) are currently investigated with a ۱۰ mm phosphate buffer, at pH = ۷ via circular dichroism (CD) and UV spectroscopy. The results showed that temperatures in the range of ۲۵oC to ۵۵oC induce a reversible structural change in the HSA structure. HSA phase transition related to physiological and pathological conditions of the body, especially fever. The conformational change observed in the HSA is accompanied by a slight conversion of its secondary structure. Acetaminophen is a papular pain killer, and HSA is used as a carrier of the drug. Hence, acetaminophen can interact with HSA. In this study of HSA - acetaminophen interaction shows that the effects of acetaminophen on the structure of HSA, prevent its phase transition. HSA-acetaminophen interaction has led to stabilization. This interaction is associated with ۸ times the kJ / mol free energy change. Structural changes in HSA due to its interaction with acetaminophen can be considered as a side effect of drugs and it may affect protein function.

کلیدواژه ها:

Human serum albumin ، Conformation ، Temperature ، Circular dichroism (CD) ، Acetaminophen.