Stability and remineralization of proteoglycan-infused dentin substrate.
Collagen
Dentin
Electron microscopy
Glycosaminoglycans
Proteoglycans
Remineralization
Journal
Dental materials : official publication of the Academy of Dental Materials
ISSN: 1879-0097
Titre abrégé: Dent Mater
Pays: England
ID NLM: 8508040
Informations de publication
Date de publication:
11 2021
11 2021
Historique:
received:
22
04
2021
revised:
09
07
2021
accepted:
03
09
2021
pubmed:
21
9
2021
medline:
16
11
2021
entrez:
20
9
2021
Statut:
ppublish
Résumé
This study tested the effects of small leucine-rich proteoglycan (SLRP) proteins on phosphoric acid (PA)-treated dentin bonding overtime and the role of such SLRPs in the remineralization potential of demineralized dentin collagen. Coronal dentin sections of human molars were used. SLRPs were either decorin (DCN) or biglycan (BGN) in core or proteoglycan form (with glycosaminoglycans, GAGs). Groups were: No treatment (control), DCN core, DCN + GAGs, BGN core, BGN + GAGs. Samples were etched with PA for 15 s and prior to application of Adper Single Bond Plus and composite buildup an aliquot of the specific SLRPs was applied over dentin. Twenty-four hours or 6 months after the bonding procedure, samples were tested for microtensile bond strength (MTBS). Debonded beams were analyzed by scanning electron microscopy (SEM). For remineralization studies, dentin blocks were fully demineralized, infused with the SLRPs, placed in artificial saliva for 2 weeks, and evaluated by transmission electron microscopy (TEM). MTBS test presented a mean of 51.4 ± 9.1 MPa in control with no statistically significant difference to DCN core (47.6 ± 8.3) and BGN core (48.3 ± 6.5). The full proteoglycan groups DCN + GAGs (27.4 ± 4.5) and BGN + GAGs (36.4 ± 13.6) showed decreased MTBS compared to control (p < 0.001). At 6 months, control or core-treated samples did not have a statistically significant difference in MTBS. However, SLRPs with GAGs showed statistically significant improvement of bonding (62.5 ± 6.0 for DCN and 52.8 ± 8.1 for BGN, p < 0.001) compared to their baseline values. SEM showed that GAGs seem to favor water retention but overtime help remineralization. TEM of demineralized dentin indicated a larger collagen fibril diameter pattern of samples treated with core proteins compared to control and a smaller diameter with DCN + GAGs in water with evidence of mineralization with DCN + GAGS, BGN core and BGN + GAGs. In conclusion, core proteins seem not to affect dentin adhesion significantly but the presence of GAGs can be detrimental to immediate bonding. However, after ageing of samples, full proteoglycans, particularly DCN, can significantly improve bonding overtime while promoting remineralization which can prove to be clinically beneficial.
Identifiants
pubmed: 34538503
pii: S0109-5641(21)00247-5
doi: 10.1016/j.dental.2021.09.003
pmc: PMC8578404
mid: NIHMS1739619
pii:
doi:
Substances chimiques
Collagen
9007-34-5
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Pagination
1724-1733Subventions
Organisme : NCI NIH HHS
ID : P30 CA016086
Pays : United States
Informations de copyright
Published by Elsevier Inc.
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