Influence of organic solvents on the furin activity

Abstract

Furin belongs to a family of calcium-dependent serine proprotein convertases, which transform the inactive protein precursors into mature polypeptides. In model experiments, we studied the effect of organic solvents such as acetone, dimethyl sulfoxide (DMSO), dioxane, isopropanol and ethanol on the furin activity. Furin was found to retain up to 88% of its initial activity in the presence of DMSO, whereas in the presence of acetone only 30%. Organic solvents formed the following decreasing sequence of their effects on furin: acetone> isopropanol> ethanol> dioxane> dimethyl sulfoxide. The relationship between the residual furin activity and solvent parameters such as relative polarity, dipole moment and log P were investigated. The effect of the organic solvent appeared not to correlate with any of the listed characteristics. Laidler-Sсatchard’s graphs, which according to a theory must be linear, demostrated non-linearity. These results indicate that not only electrostatic interactions play an important role in the studied enzymatic reaction but also other factors, e.g. hydrophobic contacts, hydrogen bonds can influence furin catalysis. This seems relevant for further research in this area.

Keywords

• activation
• furin
• furin activity
• inhibition
• organic solvents