A novel dry-bonding approach to reduce collagen degradation and optimize resin-dentin interfaces

dc.contributor.authorStape T.
dc.contributor.authorSeseogullari-Dirihan R.
dc.contributor.authorTjäderhane L.
dc.contributor.authorAbuna G.
dc.contributor.authorMartins L.
dc.contributor.authorTezvergil-Mutluay A.
dc.contributor.organizationfi=hammaslääketieteen laitos|en=Institute of Dentistry|
dc.contributor.organizationfi=tyks, vsshp|en=tyks, varha|
dc.contributor.organization-code1.2.246.10.2458963.20.64787032594
dc.converis.publication-id36893330
dc.converis.urlhttps://research.utu.fi/converis/portal/Publication/36893330
dc.date.accessioned2022-10-28T14:22:25Z
dc.date.available2022-10-28T14:22:25Z
dc.description.abstract<p>In dentistry, the wet-bonding approach relies on water to maintain demineralized collagen expanded for proper resin infiltration; nevertheless, hydrolytic instability of the resin-dentin interface is inevitable with current bonding techniques. Considering dimethyl sulfoxide’s (DMSO) ability to “biomodify” collagen and precipitate enzymes, the aim was to test whether the use of DMSO would permit adequate resin bonding to H3PO4-etched dehydrated dentin and assess its impact on collagen degradation by host-derived enzymes. Etched dentin surfaces from extracted sound human molars were randomly bonded in wet or dry conditions using aqueous or ethanolic DMSO solutions as pretreatments and bonding resins with or without DMSO. Bonded teeth were sectioned into resin-dentin slabs for confocal <i>in situ</i>zymography and beams for microtensile bond strength test. Demineralized powdered dentin was incubated in the tested DMSO -media and a hydroxyproline assay evaluated dissolution of collagen peptides. Zymography was performed on protein extracts obtained from dry and wet H3PO4-ecthed dentin powder treated with the DMSO- media. The correlative biochemical analysis demonstrated that reduction of water content during dentin hybridization by the innovative dry-bonding approaches with DMSO is effective to inactivate host-derived MMP-2 and MMP-9 and thus reduce collagen degradation while simultaneously optimizing resin-dentin bonding.<br /></p>
dc.identifier.jour-issn2045-2322
dc.identifier.olddbid187880
dc.identifier.oldhandle10024/170974
dc.identifier.urihttps://www.utupub.fi/handle/11111/43372
dc.identifier.urnURN:NBN:fi-fe2021042720256
dc.language.isoen
dc.okm.affiliatedauthorStape, Thiago
dc.okm.affiliatedauthorTezvergil-Mutluay, Arzu
dc.okm.affiliatedauthorSeseogullari Dirihan, Roda
dc.okm.affiliatedauthorDataimport, tyks, vsshp
dc.okm.discipline313 Dentistryen_GB
dc.okm.discipline313 Hammaslääketieteetfi_FI
dc.okm.internationalcopublicationinternational co-publication
dc.okm.internationalityInternational publication
dc.okm.typeA1 ScientificArticle
dc.publisherNature Publishing Group
dc.relation.articlenumber16890
dc.relation.doi10.1038/s41598-018-34726-8
dc.relation.ispartofjournalScientific Reports
dc.relation.volume8
dc.source.identifierhttps://www.utupub.fi/handle/10024/170974
dc.titleA novel dry-bonding approach to reduce collagen degradation and optimize resin-dentin interfaces
dc.year.issued2018

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