The influence of fillers and protease inhibitors in experimental resins in the protein profile of the acquired pellicle formed in situ on enamel-resin specimens

Arch Oral Biol. 2019 Dec:108:104527. doi: 10.1016/j.archoralbio.2019.104527. Epub 2019 Aug 14.

Abstract

Objective: This study evaluated the influence of the addition of fillers and/or protease inhibitors [(epigallocatechin gallate - EGCG) or (chlorhexidine - CHX)] in experimental resins in the protein profile of the acquired pellicle (AP) formed in situ on enamel-resin specimens.

Design: 324 samples of bovine enamel were prepared (6 × 6 × 2 mm). The center of each sample was added with one of the following experimental resins (Bis-GMA+TEGDMA): no filler, no inhibitor (NF-NI); filler no inhibitor (F-NI); no filler plus CHX (NF-CHX); filler plus CHX (F-CHX); no filler plus EGCG (NF-EGCG); filler plus EGCG (F-EGCG). Nine subjects used a removable jaw appliance (BISPM - Bauru in situ pellicle model) with 2 slabs from each group. The AP was formed for 120 min, in 9 days and collected with electrode filter paper soaked in 3% citric acid. The pellicles collected were processed for analysis by LC-ESI-MS/MS.

Results: A total of 140 proteins were found in the AP collected from all the substrates. Among them, 16 proteins were found in common in all the groups: 2 isoforms of Basic salivary proline-rich protein, Cystatin-S, Cystatin-AS, Cystatin-SN, Histatin-1, Ig alpha-1 chain C region, Lysozyme C, Mucin-7, Proline-rich protein 4, Protein S100-A9, Salivary acidic proline-rich phosphoprotein ½ and Statherin. Proteins with other functions, such as metabolism and transport, were also identified.

Conclusion: The composition of the experimental resins influenced the protein profile of the AP. This opens a new avenue for the development of new materials able to guide for AP engineering, thus conferring protection to the adjacent teeth.

Keywords: Acquired pellicle; Proteomics; Resin.

MeSH terms

  • Animals
  • Cattle
  • Dental Enamel* / metabolism
  • Dental Pellicle* / metabolism
  • Protease Inhibitors* / pharmacology
  • Proteins
  • Resins, Synthetic
  • Tandem Mass Spectrometry*

Substances

  • Protease Inhibitors
  • Proteins
  • Resins, Synthetic