Interaction between Silver Nanoparticles and Two Dehydrogenases: Role of Thiol Groups

Abstract

Widely used silver nanoparticles (AgNPs) are readily accessible to biological fluids and then surrounded by proteins. However, interactions between AgNPs and proteins are poorly understood. Two dehydrogenases, glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) and malate dehydrogenase (MDH), are chosen to investigate these interactions. Ag bound to thiol groups of these enzymes significantly decreases the number of free thiols available. Dose‐dependent inhibition of enzyme activities is observed in both AgNPs and Ag⁺ treatments. Based on the concentration required to inhibit 50% activity, GAPDH and MDH are 24–30 fold more sensitive to Ag⁺ than to AgNPs suggesting that the measured 4.2% Ag⁺ containing AgNPs can be responsible for the enzymes inhibition. GAPDH, with a thiol group in its active site, is more sensitive to Ag than MDH, displaying many thiol groups but none in its active site, suggesting that thiol groups at the active site strongly determines the sensitivity of enzymes toward AgNPs. In contrast, the dramatic changes of circular dichroism spectra show that the global secondary structure of MDH under AgNPs treatment is more altered than that of GAPDH. In summary, this study shows that the thiol groups and their location on these dehydrogenases are crucial for the AgNPs effects.