Cross-linked dry bonding: A new etch-and-rinse technique.

OBJECTIVE: To determine if acid-etched, cross-linked dentin can be dehydrated without lowering bond strength below that of cross-linked wet-bonded dentin in vitro. METHODS: Using extracted human third molars, control acid-etched dentin was bonded with Single Bond Plus, using either the wet- or dry-bonding technique. Experimental acid-etched dentin was treated with 5mass% grape seed extract (GSE) in different solvents for 1min before undergoing wet vs dry resin-dentin bonding with Single Bond Plus. Completely demineralized dentin beams were treated with 5% GSE for 0, 1 or 10min, before measuring stiffness by 3-point flexure. Other completely demineralized beams were treated similarly and then incubated in buffer for 1 week to measure the collagen solubilization by endogenous dentin proteases. RESULTS: 24h microtensile bond strengths (µTBS) in wet and dry controls were 53.5±3.6 and 9.4±1.8MPa, respectively (p<0.05). 5% GSE in water gave µTBS of 53.7±3.4 and 39.1±9.7MPa (p<0.05), respectively, while 5% GSE in ethanol gave µTBS of 51.2±2.3 and 35.3±2.0MPa (p<0.05). 5% GSE in 5% EtOH/95% water gave wet and dry µTBS of 53.0±2.3 and 55.7±5.1MPa (p>0.05). Cross-linking demineralized dentin with 5% GSE increased stiffness of dentin and decreased collagen degradation (p<0.05). SIGNIFICANCE: 5% GSE pretreatment of acid-etched dentin for 1min permits the dentin to be completely air-dried without lowering bond strength.

Investigation of ethanol infiltration into demineralized dentin collagen fibrils using molecular dynamics simulations.

The purpose of this study is to investigate the interaction of neat ethanol with bound and non-bound water in completely demineralized dentin that is fully hydrated, using molecular dynamics (MD) simulation method. The key to creating ideal resin-dentin bonds is the removal of residual free water layers and its replacement by ethanol solvent in which resin monomers are soluble, using the ethanol wet-bonding technique. The test null hypotheses were that ethanol cannot remove any collagen-bound water, and that ethanol cannot infiltrate into the spacing between collagen triple helix due to narrow interlayer spacing. Collagen fibrillar structures of overlap and gap regions were constructed by aligning the collagen triple helix of infinite length in hexagonal packing. Three layers of the water molecules were specified as the layers of 0.15-0.22nm, 0.22-0.43nm and 0.43-0.63nm from collagen atoms by investigating the water distribution surrounding collagen molecules. Our simulation results show that ethanol molecules infiltrated into the intermolecular spacing in the gap region, which increased due to the lateral shrinkage of the collagen structures in contact with ethanol solution, while there was no ethanol infiltration observed in the overlap region. Infiltrated ethanol molecules in the gap region removed residual water molecules via modifying mostly the third water layer (50% decrease), which would be considered as a loosely-bound water layer. The first and second hydration layers, which would be considered as tightly bound water layers, were not removed by the ethanol molecules, thus maintaining the helical structures of the collagen molecules.