Oxidative modifications and structural changes of human serum albumin in response to air dielectric barrier discharge plasma

In this work, the air dielectric barrier discharge plasma was applied to a model of protein human serum albumin to explore plasma-mediated protein damage from a biomolecular perspective. Carbonylation and side chain modifications of protein in solution were observed by Fourier transform infrared (FT-IR) spectroscopy and mass spectrometry (MS). Protein backbone cleavage is proved by Bradford assay, sodium dodecyl sulphate–polyacrylamide gel electrophoresis, and MS. Typical fragments are in the range of 10–12 kDa. The decrease in α-helix and increase in β-sheet indicated by FT-IR are major protein secondary structure changes. Accordingly, a whole map of protein oxidative damage and structural changes in response to the plasma was postulated.