Abstract

Considering the improvement of biomaterials that facilitate atraumatic restorative techniques in dentistry, a papain-based gel can be used in the chemomechanical removal of decayed dental tissue. However, there is no information regarding the influence of this gel on the structure of sound collagen. The aim of the present study was to investigate the adsorption of a papain-based gel (PapacarieTM) to collagen and determine collagen integrity after treatment. A pilot study was first performed with 10 samples of type I collagen membrane obtained from bovine Achilles deep tendon to compare the influence of hydration (Milli-Q water) on infrared bands of collagen. In a further experiment, 10 samples of type I collagen membrane were used to evaluate the effects of PapacarieTM on the collagen microstructure. All analyses were performed using the attenuated total reflectance technique of Fourier transform infrared (ATR-FTIR). The results demonstrated that the application of PapacarieTM does not lead to the degradation of collagen and this product can be safely used in minimally invasive dentistry. As the integrity of sound collagen is preserved after the application of the papain-based gel, this product is indicated for the selective removal of infected dentin, leaving the affected dentin intact and capable of re-mineralization.

Highlights

  • In dentistry, minimally invasive treatment is based on the selective removal of decayed tissue, which has led to a transformation in the paradigm of restorative treatment for tooth decay, allowing the maximum preservation of sound tooth structure and tissue capable of re-mineralization[1,2]

  • The treatment of the dentinal surface and the resulting characteristics of the dentinal substrate are important to adhesion and affect the performance of composite resin restorations, as adhesion is mainly based on micromechanical retention by the formation of a hybrid layer and resin tags within the dentinal tubules

  • To clarify whether PapacarieTM degrades intact collagen and alters the chemical structure of this protein, the aim of the present study was to evaluate the structure of type-I collagen under the action of the papain-based gel using the attenuated total reflectance technique of Fourier transform infrared (ATR-FTIR) spectroscopy

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Summary

Introduction

Minimally invasive treatment is based on the selective removal of decayed tissue, which has led to a transformation in the paradigm of restorative treatment for tooth decay, allowing the maximum preservation of sound tooth structure and tissue capable of re-mineralization[1,2]. The necrotic surface layer and underlying infected dentin, which has a large number of bacteria, is completely de-mineralized, has a disorganized collagen structure and must be removed. The aim of the partial removal of carious lesions in minimally invasive techniques is to leave the affected dentin, which allows the preservation and re-mineralization of the dental structure and avoids pulp exposure[6,7]. The application of chemomechanical methods, such as papain-based gel, on the sound surrounding walls should not alter the mechanical properties of collagen fibers. Despite their common use, direct dental composite resin systems have short durability (approximately 5 to 8 years). A stable bond between the adhesive system and collagen fibers forming the hybrid layer remains a challenge in restorative dentistry

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