Logo del repository
  1. Home
 
Opzioni

Mechanisms of degradation of the hybrid layer in adhesive dentistry and therapeutic agents to improve bond durability - A literature review

FRASSETTO, ANDREA
•
Breschi, Lorenzo
•
TURCO, GIANLUCA
altro
CADENARO, MILENA
2016
  • journal article

Periodico
DENTAL MATERIALS
Abstract
Success in adhesive dentistry means long lasting restorations. However, there is substantial evidence that this ideal objective is not always achieved. Current research in this field aims at increasing the durability of resin-dentin bonds. The objective of this paper is to examine the fundamental processes responsible for the aging mechanisms involved in the degradation of resin-bonded interfaces and the potential approaches to prevent and counteract this degradation. METHODS: PubMed searches on the hybrid layer degradation were carried out. Keywords were chosen to assess hybrid layer degradation for providing up-dated information on the basis of scientific coherence with the research objective. Approaches to prevent and counteract this degradation were also reviewed. RESULTS: 148 peer-review articles in the English language between 1982 and 2015 were reviewed. Literature shows that resin-dentin bond degradation is a complex process, involving the hydrolysis of both the resin and the collagen fibril phases contained within the hybrid layer. Collagen fibers become vulnerable to mechanical and hydraulic fatigue, as well as degradation by host-derived proteases with collagenolytic activity (matrix metalloproteinases and cysteine cathepsins). Inhibition of the collagenolytic activity and the use of cross-linking agents are the two main strategies to increase the resistance of the hybrid layer to enzymatic degradation. SIGNIFICANCE: This review analyzes the issues regarding the durability of the adhesive interface, and the techniques to create stable resin-dentin bonds able to resist the collagenolytic hydrolysis that are currently studied.
DOI
10.1016/j.dental.2015.11.007
WOS
WOS:000370808400004
Archivio
http://hdl.handle.net/11368/2869765
info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84957849616
http://www.sciencedirect.com/science/article/pii/S0109564115004650
Diritti
open access
FVG url
https://arts.units.it/request-item?handle=11368/2869765
Soggetti
  • Collagen

  • Cross-linking agent

  • Dentin

  • EDC

  • Hybrid layer degradat...

  • Metalloproteinase

  • Dentistry (all)

  • Materials Science (al...

  • Mechanics of Material...

Web of Science© citazioni
232
Data di acquisizione
Mar 25, 2024
Visualizzazioni
1
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