The importance of size-exclusion characteristics of type i collagen in bonding to dentin matrices

M. Takahashi, M. Nakajima, J. Tagami, D. L.S. Scheffel, R. M. Carvalho, A. Mazzoni, M. Cadenaro, A. Tezvergil-Mutluay, L. Breschi, L. Tjäderhane, S. S. Jang, F. R. Tay, K. A. Agee, D. H. Pashley

Research output: Contribution to journalArticlepeer-review

61 Scopus citations


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.

Original languageEnglish
Pages (from-to)9522-9528
Number of pages7
JournalActa Biomaterialia
Issue number12
StatePublished - Dec 2013

Bibliographical note

Funding Information:
This work was supported, in part, by R01 DE015306 from the NIDCR to D.P. (PI) and by the King Abdulazis University which supports D.H.P. as a Highly Cited Scholar. The authors are grateful to Mrs Michelle Barnes for her secretarial support.


  • Collagen
  • Collagen water
  • Mineralized collagen
  • Resin-dentin bonding
  • Size-exclusion

ASJC Scopus subject areas

  • Biotechnology
  • Biomaterials
  • Biochemistry
  • Biomedical Engineering
  • Molecular Biology


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