IADR Abstract Archives
Proteomic Analysis Of The Salivary Pellicle Formed On Implant Surfaces
Objectives: To analyze differences in the proteome of the salivary pellicles formed under in situ conditions on titanium dental implant surfaces with different roughness and wettability by using a proteomic approach.
Methods: Salivary pellicles formed on smooth (TiPT), and rough (TiSLA) dental titanium surfaces were quantitatively and qualitatively evaluated; dental enamel was used as a reference substrate. The adsorbed salivary proteins were quantified by Bicinchoninic Acid assays, while the pellicle’s proteome was analyzed by Nano-LC-MS/MS (nano mass spectrometry).
Results: Enamel surfaces exhibited the lowest values of Ra (0.06 µm), WCA (43.8°), and Ip (3.60), while TiPT surfaces (Ra of 0.45 µm) showed WCA of 92.4° and Ip of 4.27. The TiSLA surfaces had a Ra of 3.2 µm, a WCA of 131.7°, and pI of 4.48. After the in situ incubation, protein levels of 5.6, 2.5, and 9.1 µg/mL were quantified from the detached salivary pellicles formed on the enamel, TiPT, and TiSLA surfaces, respectively. Using Nano-LC-MS/MS, a total of 597 proteins were identified on the test substrates; 49 proteins were exclusively identified on enamel, 43 proteins were identified only on the TiPT, and 226 proteins were adsorbed solely on the TiSLA substrates.
Conclusions: The amount and the identity of the salivary proteome detected on the Ti surfaces were directly affected by the physicochemical characteristics of the substrates, confirming the high selectivity of the protein pellicle formed on a surface once exposed in the oral cavity.
Methods: Salivary pellicles formed on smooth (TiPT), and rough (TiSLA) dental titanium surfaces were quantitatively and qualitatively evaluated; dental enamel was used as a reference substrate. The adsorbed salivary proteins were quantified by Bicinchoninic Acid assays, while the pellicle’s proteome was analyzed by Nano-LC-MS/MS (nano mass spectrometry).
Results: Enamel surfaces exhibited the lowest values of Ra (0.06 µm), WCA (43.8°), and Ip (3.60), while TiPT surfaces (Ra of 0.45 µm) showed WCA of 92.4° and Ip of 4.27. The TiSLA surfaces had a Ra of 3.2 µm, a WCA of 131.7°, and pI of 4.48. After the in situ incubation, protein levels of 5.6, 2.5, and 9.1 µg/mL were quantified from the detached salivary pellicles formed on the enamel, TiPT, and TiSLA surfaces, respectively. Using Nano-LC-MS/MS, a total of 597 proteins were identified on the test substrates; 49 proteins were exclusively identified on enamel, 43 proteins were identified only on the TiPT, and 226 proteins were adsorbed solely on the TiSLA substrates.
Conclusions: The amount and the identity of the salivary proteome detected on the Ti surfaces were directly affected by the physicochemical characteristics of the substrates, confirming the high selectivity of the protein pellicle formed on a surface once exposed in the oral cavity.
