Research on Specroscopy of Cu(II) on Peroxynitrite Nitrifying Fibrinogen

Many studies have showed that peroxynitrite-mediated injury on fibrinogen has some relations with Thrombotic diseases. However there are few reports about structural changes of nitrified fibrinogen when metallic ions exist in this reaction. In this study, we use methods of FTIR-ATR spectra and 3D Fluorescence spectra to study the structural changes on fibrinogen after nitration and oxidation damages caused by ONOO- with Cu(Π) exist. Our results showed that Cu(Π) enhance the production of 3-nitrotyrosine in proteins, The FTIR spectra indicated that the α-helix in fibrinogen reacted with ONOO- by adding Cu(Π) decreases from 38.03 % to 28.5 %, whereas β-sheet increases from 29.89% to 43.99 %. Consequently, Cu(Π) could promote Fg nitration with its concentration dependence.