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

Author(s)

Pela, Vinicius Taioqui ^[1] ; Prakki, Anuradha ^[2] ; Wang, Linda ^[3] ; Silva Ventura, Talita Mendes ^[3] ; de Souza E Silva, Cintia Maria ^[3] ; Silva Cassiano, Luiza Paula ^[3] ; Freitas Brianezzi, Leticia Ferreira ^[3] ; Leite, Aline Lima ^[3] ; Rabelo Buzalaf, Marilia Afonso ^[3]

Affiliation

^[1] Univ Fed Sao Carlos, Dept Genet & Evolut, Sao Carlos, SP - Brazil

^[2] Univ Toronto, Fac Dent, Dept Clin Sci, Toronto, ON - Canada

^[3] Univ Sao Paulo, Bauru Sch Dent, Dept Biol Sci, Al Octavio Pinheiro Brisolla 9-75, BR-17012901 Bauru, SP - Brazil

• Document type: Journal article
• Source: ARCHIVES OF ORAL BIOLOGY; v. 108, DEC 2019.
• Web of Science Citations: 1

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 x 6 x 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 5100 A9, Salivary acidic proline-rich phosphoprotein 1/2 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. (AU)

• FAPESP's process: 14/25599-5 - PROTEOMIC ANALYSIS OF ACQUIRED PELLICLE FORMED ON EXPERIMENTAL COMPOSITE RESINS CONTAINING OR NOT FILLER AND/OR PROTEASE INHIBITORS
• Grantee: Vinícius Taioqui Pelá
• Support Opportunities: Scholarships in Brazil - Master