title: Quantitative contribution of the collagen network in dentin hybridization.
abstract: OBJECTIVE
  To determine the quantitative contribution of dentin hybridization to bonded assembly strength and demonstrate the micromorphology of the interface with and without collagen present.
  
  
  METHODS
  Four groups of 10 molar teeth were finished to a 320 grit dentin smear layer. Two groups served as controls and two experimental groups were subjected to collagenase digestion of the collagen exposed by acid conditioning. All-Bond 2 and Amalgambond were used to bond Bisfil and Epic resin composite, respectively. Stored in water at 37 degrees C for 24 hours the assemblies were tested in a shear mode at a crosshead speed of 5 mm/minute. Means and standard deviations were subjected to analysis for statistical significance. Twenty four teeth in four groups were examined by scanning (SEM) and transmission electron microscopy (TEM) for the relationship between resin and conditioned dentin with and without the collagen network.
  
  
  RESULTS
  All-Bond 2 and Amalgambond controls were 28.41 +/- 3.9 and 19.04 +/- 5.96 MPa, collagenase-treated groups scored 26.43 +/- 2.90 and 19.70 +/- 4.25 MPa respectively. No significant difference existed between the control and experimental groups. SEM showed an intertubular collagen network with patent tubules and a pronounced porous, irregular dentin topography following collagen digestion. A distinct hybrid zone and tubular penetration was observed but the collagenase-treated specimens showed only resin in the tubules and their lateral extensions. TEM confirmed the absence of a distinct hybrid zone in the collagenase groups with a tight, gap-free junction between the resin and the undemineralized dentin. An electron dense zone (< 50 nm) at the leading edge of conditioning was observed for All-Bond 2 and Amalgambond groups. It was concluded that the resin-reinforced or hybridized, collagenous network does not detract from, nor contribute any significant quantitative value per se to dentin bonding with the systems tested.
authors.affiliation: Department of Oral Biology and Pathology, School of Dental Medicine, SUNY at Stony Brook 11794-8702, USA.
authors.forename: A J
authors.initials: AJ
authors.lastname: Gwinnett
authors.forename: F R
authors.initials: FR
authors.lastname: Tay
authors.forename: K M
authors.initials: KM
authors.lastname: Pang
authors.forename: S H
authors.initials: SH
authors.lastname: Wei
mesh_terms: D000134:Acid Etching, Dental; D000704:Analysis of Variance; D003094:Collagen; D017364:Collagenases; D003188:Composite Resins; D001840:Dental Bonding; D003804:Dentin / Q000737:chemistry* / Q000648:ultrastructure; D017220:Dentin-Bonding Agents; D008422:Materials Testing; D008689:Methacrylates; D008855:Microscopy, Electron, Scanning; D013499:Surface Properties; D017001:Tooth Demineralization
chemical_list: C074864:All-Bond system; C070606:Amalgambond; D003188:Composite Resins; D017220:Dentin-Bonding Agents; D008689:Methacrylates; D003094:Collagen; D017364:Collagenases