Logo del repository
  1. Home
 
Opzioni

Dentin bonding systems: From dentin collagen structure to bond preservation and clinical applications

Breschi, Lorenzo
•
Maravic, Tatjana
•
Cunha, Sandra Ribeiro
altro
Mazzoni, Annalisa
2018
  • journal article

Periodico
DENTAL MATERIALS
Abstract
Objectives. Efforts towards achieving durable resin-dentin bonds have been made for decades, including the understanding of the mechanisms underlying hybrid layer (HL) degradation, manufacturing of improved adhesive systems, as well as developing strategies for the preservation of the HL. Methods. This study critically discusses the available peer-reviewed research concerning the formation and preservation of the HL, the mechanisms that lead to the degradation of the HL as well as the strategies to prevent it. Results. The degradation of the HL occurs through two main mechanisms: the enzymatic degradation of its collagen fibrils, and the leaching of the resin from the HL. They are enabled by residual unbound water between the denuded collagen fibrils, trapped at the bottom of the HL. Consequently, endogenous dentinal enzymes, such as the matrix metalloproteinases (MMPs) and cysteine cathepsins are activated and can degrade the denuded collagen matrix. Strategies for the preservation of the HL over time have been developed, and they entail the removal of the unbound water from the gaps between the collagen fibrils as well as different modes of silencing endogenous enzymatic activity. Significance. Although there are many more hurdles to be crossed in the field of adhesive dentistry, impressive progress has been achieved so far, and the vast amount of available research on the topic is an indicator of the importance of this matter and of the great efforts of researchers and dental material companies to reach a new level in the quality and longevity of resin-dentin bonds. (C) 2017 The Academy of Dental Materials. Published by Elsevier Ltd. All rights reserved.
DOI
10.1016/j.dental.2017.11.005
WOS
WOS:000418642500009
Archivio
http://hdl.handle.net/11368/2916002
info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85034849777
https://www.sciencedirect.com/science/article/pii/S010956411731120X?via%3Dihub
Diritti
open access
license:digital rights management non definito
license:digital rights management non definito
FVG url
https://arts.units.it/request-item?handle=11368/2916002
Soggetti
  • Collagen

  • Cross-linking agent

  • Dentin

  • Dentin bonding system...

  • Enzyme inhibition

  • Hybrid layer

  • Metalloproteinase

  • Materials Science (al...

  • Dentistry (all)

  • Mechanics of Material...

Scopus© citazioni
156
Data di acquisizione
Jun 7, 2022
Vedi dettagli
Web of Science© citazioni
259
Data di acquisizione
Mar 20, 2024
Visualizzazioni
2
Data di acquisizione
Apr 19, 2024
Vedi dettagli
google-scholar
Get Involved!
  • Source Code
  • Documentation
  • Slack Channel
Make it your own

DSpace-CRIS can be extensively configured to meet your needs. Decide which information need to be collected and available with fine-grained security. Start updating the theme to match your nstitution's web identity.

Need professional help?

The original creators of DSpace-CRIS at 4Science can take your project to the next level, get in touch!

Realizzato con Software DSpace-CRIS - Estensione mantenuta e ottimizzata da 4Science

  • Impostazioni dei cookie
  • Informativa sulla privacy
  • Accordo con l'utente finale
  • Invia il tuo Feedback