Comparative evaluation of 5-15-kDa salivary proteins from patients with different oral diseases by MALDI-TOF/TOF mass spectrometry

The present study aimed to determine the potential use of matrix-assisted laser desorption/ionization with time-of-flight/time-of-flight mass spectrometry (MALDI-TOF/TOF MS) for analyzing specific patterns of mass signals of low-molecular-weight proteins in saliva from patients with different oral diseases. Unstimulated whole saliva samples were collected from healthy subjects (n = 30) and patients with oral diseases including oral cancer (n = 30), oral lichen planus (n = 30), and chronic periodontitis (n = 30). Proteomic profiles of 5,000-15,000-Da salivary proteins were evaluated by MALDI-TOF/TOF MS. Quantification of mass signals was performed by FlexAnalysis and ClinProTool software. In oral cancer, the percentages of mass signals at 5,592.26 and 8,301.46 Da were significantly increased as compared with other groups (p = 0.002 and p = 0.030, respectively). In oral lichen planus, the percentages of mass signals at 12,964.55 and 13,279.08 Da were significantly increased as compared with other groups (p < 0.001, and p < 0.001, respectively). In chronic periodontitis, the percentages of mass signals at 5,835.73 and 9,801.83 Da were significantly decreased as compared with other groups (p = 0.003 and p = 0.005, respectively). The present study demonstrated a potential use of MALDI-TOF/TOF as a rapid screening method to differentiate one oral disease from others by identifying specific patterns of mass signals in saliva from patients. However, MALDI-TOF/TOF has several limitations regarding the identification of the candidate mass signals. MALDI-TOF/TOF MS can be used as a rapid screening method to differentiate one oral disease from others with a caution concerning peptide identity.