Investigation of the Interaction between N-Acetyl-L-Cysteine and Ovalbumin by Spectroscopic Studies, Molecular Docking Simulation, and Real-Time Quartz Crystal Microbalance with Dissipation
This study investigated the interaction between N-acetyl-L-cysteine (NAC) and ovalbumin (OVA) using multispectroscopic technology, molecular docking, and quartz crystal microbalance with dissipation (QCM-D). Fluorescence intensity and UV absorption of OVA were decreased substantially upon the addition of NAC. The calculated K-q values were obtained at 298, 304, and 310 K for 13.48, 15.59, and 17.50 (x 10(12) L mol(-1)), respectively, suggesting that the static quenching was dominated. Thermodynamic parameters such as Delta H (-150.58 kJ mol(-1)), Delta S (-433.51 J mol(-1) K-1), and Delta G values (-21.39 kJ mol(-1)), combined with molecular docking and QCM-D data, showed that the interaction was spontaneous and van der Waals and hydrogen bonding were identified as the main driving forces. FTIR and CD results showed that the alpha-helix content of OVA increased from 2.8 to 22.9%, and the beta-sheet decreased from 0.2 to 21.9% in the presence of 5 and 10 mu M NAC, respectively, compared to the pure OVA, respectively.
