The importance of size-exclusion characteristics of type I collagen in bonding to dentin matrices |
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Authors: | M Takahashi M Nakajima J Tagami DLS Scheffel RM Carvalho A Mazzoni M Cadenaro A Tezvergil-Mutluay L Breschi L Tjäderhane SS Jang FR Tay KA Agee DH Pashley |
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Institution: | 1. Department of Cariology and Operative Dentistry, Tokyo Medical and Dental University, Tokyo, Japan;2. Department of Orthodontics and Pediatric Dentistry, Universidade Estadual Paulista-UNESP, Araraquara Dental School, Araraquara, São Paulo, Brazil;3. Department of Oral Science, School of Dentistry, University of British Columbia, Vancouver, British Columbia, Canada;4. Department of SAU&FAL, University of Bologna, Bologna, Italy;5. Department of Biomedicine, Unit of Dental Sciences and Biomaterials, University of Trieste, Trieste, Italy;6. Adhesive Dentistry Research Group, Institute of Dentistry, University of Turku, Turku, Finland;7. Institute of Dentistry, University of Oulu and Oulu University Hospital, Oulu;8. Institute of Dentistry, University of Turku, Turku, Finland;9. Department of Materials Science Engineering, Georgia Institute of Technology, Atlanta, GA, USA;10. Department of Oral Biology, College of Dental Medicine, Georgia Regents University, Augusta, GA, USA |
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Abstract: | The mineral phase of dentin is located primarily within collagen fibrils. During development, bone or dentin collagen fibrils are formed first and then water within the fibril is replaced with apatite crystallites. Mineralized collagen contains very little water. During dentin bonding, acid-etching of mineralized dentin solubilizes the mineral crystallites and replaces them with water. During the infiltration phase of dentin bonding, adhesive comonomers are supposed to replace all of the collagen water with adhesive monomers that are then polymerized into copolymers. The authors of a recently published review suggested that dental monomers were too large to enter and displace water from collagen fibrils. If that were true, the endogenous proteases bound to dentin collagen could be responsible for unimpeded collagen degradation that is responsible for the poor durability of resin–dentin bonds. The current work studied the size–exclusion characteristics of dentin collagen, using a gel-filtration-like column chromatography technique, using dentin powder instead of Sephadex. The elution volumes of test molecules, including adhesive monomers, revealed that adhesive monomers smaller than ~1000 Da can freely diffuse into collagen water, while molecules of 10,000 Da begin to be excluded, and bovine serum albumin (66,000 Da) was fully excluded. These results validate the concept that dental monomers can permeate between collagen molecules during infiltration by etch-and-rinse adhesives in water-saturated matrices. |
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Keywords: | Size-exclusion Collagen Mineralized collagen Collagen water Resin–dentin bonding |
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