Investigating the effect of atmospheric plasma on protein fibrinogen: Spectroscopic and biophysical analysis

Abstract

AbstractCold atmospheric plasma (CAP) has gained significance in recent years and different prospects of it have been studied widely owing to its effectiveness and eco‐friendly nature. CAP has been used extensively in wound healing. However, a detailed understanding of the interaction of the CAP with different protein macromolecules present in our body is essential. In this study, we emphasize how CAP affects the protein fibrinogen. Fibrinogen is a major protein involved in blood clotting and the major protein in the blood. Numerous spectroscopic investigations have been done including UV spectroscopy, fluorescence spectroscopy, dynamic light scattering (DLS), and Zeta. This work shines a light on protein self‐assembly to bring the future possibilities of bio‐medicine with CAP treatment. Fibrinogen undergoes structural changes around tryptophan residue as evidenced by UV spectroscopy and quenching in fluorescence spectroscopy. The order of the fluorescence quenching is Oxygen > Helium > Argon gas plasma. 2,4‐dinitrophenylhydrazine (DNPH) assay supports fluorescence studies as more protein carbonyls are formed in the case of argon and oxygen gas plasma. DLS and Zeta potential measurements prove that the protein Fibrinogen undergoes a self‐assembly process to form organized assemblies in the presence of a plasma jet. Reactive oxygen and reactive nitrogen species produced in the plasma have been evaluated using various assays and correlated with the other studies. This study will help understand protein fibrinogen's self‐assembly process and pave the way for the CAP application in wound healing.