Interactions Of Zinc Aqua Complexes With Ovalbumin At The Forefront Of The Zn2+/Zno-Ovo Hybrid Complex Formation Mechanism

The present research is focused on experimental and computational mechanistic study of the nanocomplexes formation through Zn-(aq)(2+)-ovalbumin (OVA) binding. The determination of processes occurring at Zn-(aq)(2+)-OVA interfaces and mechanism of hybrid complexes formation involved the modeling of kinetics and isotherm of Zn-(aq)(2+) binding. Scanning electron microscopy, energy-dispersive X-ray analysis and X-ray diffraction were employed to characterize the nano-crystalline structure and morphology of the Zn2+/ZnO-OVO hybrid complex. Formation of hybrid complex was monitored using Fourier transform infrared spectroscopy. Specific Zn-(aq)(2+) binding sites were pointed using MD simulations. Large-scale MD analysis was carried out to sample conformational space of the formed Zn-(aq)(2+)-OVA complexes. Density functional theory (DFT) calculations were used to investigate the structures of the interaction complexes between zinc(II) and Asp/Glu - and predict their respective IR spectra, and for mechanistic modeling of oxidation processes involved in the formation and stabilization Zn2+/ZnO-OVO hybrid complex. Negatively charged ovalbumin surface was locally neutralized through rapid Zn-(aq)(2+) adsorption and formation of monolayers via 1:1 Asp(-)/Glu(-)/-Zn-(aq)(2+) complexes. The ovalbumin monomer species began to agglomerate, stabilized with Asp(-)/Glu(-)Zn((aq))(2+)-Glu /Asp(-) interface complexes that promoted the formation of nanocomplexes. Finally, antimicrobial assays have shown that Zn2+/ ZnO-OVO hybrid complex exhibit an inhibition effect against bacteria (A. baumanii, K. pneumonia) and yeast (C. albicans) strains.