Comprehensive identification of the binding sites of cisplatin in hen egg white lysozyme

摘要: Platinum drugs have become one of the most important kinds chemotherapy agents, and interactions these with proteins play very roles in their side effects drug resistance. However, it is still a challenge to determine binding sites platinum multiple disulfide bonds stable three-dimensional structures using mass spectrometry. Here, interaction between cisplatin hen egg white lysozyme (HEWL), multi-disulfide-bond-containing protein structure, was investigated Fourier transform ion cyclotron resonance Typical bond reduction dithiothreitol/tris(2-carboxyethyl)phosphine before trypsin digestion destroyed HEWL, no platination were found. Efficient methods for HEWL–cisplatin adducts developed avoid loss protein. At 55 °C, platinated HEWL digested directly by 6 h, peptides observed. In 60 % acetonitrile, time shortened 2 h, addition, greatly accelerated reaction cisplatin, potential reduced could be easily recognized. On basis above-mentioned methods, first identified