Limits...
The dentin organic matrix - limitations of restorative dentistry hidden on the nanometer scale.

Bertassoni LE, Orgel JP, Antipova O, Swain MV - Acta Biomater (2012)

Bottom Line: Research has shown, however, that this interaction imposes less than desirable long-term prospects for current resin-based dental restorations.Finally, we discuss the relation of these complexly assembled nanostructures with the protease degradative processes driving the low durability of current resin-based dental restorations.We argue in favour of the structural limitations that these complexly organized and inherently hydrated organic structures may impose on the clinical prospects of current hydrophobic and hydrolyzable dental polymers that establish ultrafine contact with the tooth substrate.

View Article: PubMed Central - PubMed

Affiliation: Biomaterials Science Research Unit, Faculty of Dentistry, University of Sydney, United Dental Hospital, NSW, Australia. luiz.bertassoni@sydney.edu.au

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Schematic representation of proteoglycan attached to the collagen surface (not to scale). (A) Monomeric model of decorin based on the available crystal structure of the dimeric protein core [145]. The association of decorin with the collagen surface is based on a recently proposed model [48]. The glycosaminoglycan side-chain, based on the structure of chondroitin 4-sulfate [146] is positioned in a hypothetical region of the decorin protein core with associated ions. All molecular structures are available from the National Center for Biotechnology Information structure database (http://www.ncbi.nlm.nih.gov). (B) A not to scale schematic sketch of the interfibrillar supramolecular assemblies that interconnect collagen fibrils: (1) collagen fibril; (2) decorin protein core; (3) chondroitin 4-sulfate glycosaminoglycan. The known periodicity of these interfibrillar aggregates in register with the gap zones of collagen fibrils, present in most connective tissues, remains uncertain for mineralized tissues. (C) A high magnification image of a sample of acid-soluble collagen and decorin treated with cupromeronic blue, which reacts with glycosaminoglycans and demonstrates their assembly as interfibrillar co-aggregates (arrows) [127].
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f0035: Schematic representation of proteoglycan attached to the collagen surface (not to scale). (A) Monomeric model of decorin based on the available crystal structure of the dimeric protein core [145]. The association of decorin with the collagen surface is based on a recently proposed model [48]. The glycosaminoglycan side-chain, based on the structure of chondroitin 4-sulfate [146] is positioned in a hypothetical region of the decorin protein core with associated ions. All molecular structures are available from the National Center for Biotechnology Information structure database (http://www.ncbi.nlm.nih.gov). (B) A not to scale schematic sketch of the interfibrillar supramolecular assemblies that interconnect collagen fibrils: (1) collagen fibril; (2) decorin protein core; (3) chondroitin 4-sulfate glycosaminoglycan. The known periodicity of these interfibrillar aggregates in register with the gap zones of collagen fibrils, present in most connective tissues, remains uncertain for mineralized tissues. (C) A high magnification image of a sample of acid-soluble collagen and decorin treated with cupromeronic blue, which reacts with glycosaminoglycans and demonstrates their assembly as interfibrillar co-aggregates (arrows) [127].

Mentions: An improved understanding of the specific nanostructural interaction of proteoglycans with polymeric dental materials requires a critical reappraisal of proteoglycans as a biological entity and of their interaction with the collagen fibril surface [13,131] (Fig. 7). Decorin and biglycan, two members of the small leucine-rich repeat (SLRP) family, are the proteoglycans predominantly expressed in dentin [28]. It has been shown that proteoglycans retain a protein core that adopts a folded helical configuration stabilized by hydrogen bonds and hydrophobic and electrostatic interactions [132], which has also been suggested to bind to four or more collagen microfibrils via an array of hydrogen bonds (particularly decorin) (Fig. 7) [48].


The dentin organic matrix - limitations of restorative dentistry hidden on the nanometer scale.

Bertassoni LE, Orgel JP, Antipova O, Swain MV - Acta Biomater (2012)

Schematic representation of proteoglycan attached to the collagen surface (not to scale). (A) Monomeric model of decorin based on the available crystal structure of the dimeric protein core [145]. The association of decorin with the collagen surface is based on a recently proposed model [48]. The glycosaminoglycan side-chain, based on the structure of chondroitin 4-sulfate [146] is positioned in a hypothetical region of the decorin protein core with associated ions. All molecular structures are available from the National Center for Biotechnology Information structure database (http://www.ncbi.nlm.nih.gov). (B) A not to scale schematic sketch of the interfibrillar supramolecular assemblies that interconnect collagen fibrils: (1) collagen fibril; (2) decorin protein core; (3) chondroitin 4-sulfate glycosaminoglycan. The known periodicity of these interfibrillar aggregates in register with the gap zones of collagen fibrils, present in most connective tissues, remains uncertain for mineralized tissues. (C) A high magnification image of a sample of acid-soluble collagen and decorin treated with cupromeronic blue, which reacts with glycosaminoglycans and demonstrates their assembly as interfibrillar co-aggregates (arrows) [127].
© Copyright Policy
Related In: Results  -  Collection

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Show All Figures
getmorefigures.php?uid=PMC3473357&req=5

f0035: Schematic representation of proteoglycan attached to the collagen surface (not to scale). (A) Monomeric model of decorin based on the available crystal structure of the dimeric protein core [145]. The association of decorin with the collagen surface is based on a recently proposed model [48]. The glycosaminoglycan side-chain, based on the structure of chondroitin 4-sulfate [146] is positioned in a hypothetical region of the decorin protein core with associated ions. All molecular structures are available from the National Center for Biotechnology Information structure database (http://www.ncbi.nlm.nih.gov). (B) A not to scale schematic sketch of the interfibrillar supramolecular assemblies that interconnect collagen fibrils: (1) collagen fibril; (2) decorin protein core; (3) chondroitin 4-sulfate glycosaminoglycan. The known periodicity of these interfibrillar aggregates in register with the gap zones of collagen fibrils, present in most connective tissues, remains uncertain for mineralized tissues. (C) A high magnification image of a sample of acid-soluble collagen and decorin treated with cupromeronic blue, which reacts with glycosaminoglycans and demonstrates their assembly as interfibrillar co-aggregates (arrows) [127].
Mentions: An improved understanding of the specific nanostructural interaction of proteoglycans with polymeric dental materials requires a critical reappraisal of proteoglycans as a biological entity and of their interaction with the collagen fibril surface [13,131] (Fig. 7). Decorin and biglycan, two members of the small leucine-rich repeat (SLRP) family, are the proteoglycans predominantly expressed in dentin [28]. It has been shown that proteoglycans retain a protein core that adopts a folded helical configuration stabilized by hydrogen bonds and hydrophobic and electrostatic interactions [132], which has also been suggested to bind to four or more collagen microfibrils via an array of hydrogen bonds (particularly decorin) (Fig. 7) [48].

Bottom Line: Research has shown, however, that this interaction imposes less than desirable long-term prospects for current resin-based dental restorations.Finally, we discuss the relation of these complexly assembled nanostructures with the protease degradative processes driving the low durability of current resin-based dental restorations.We argue in favour of the structural limitations that these complexly organized and inherently hydrated organic structures may impose on the clinical prospects of current hydrophobic and hydrolyzable dental polymers that establish ultrafine contact with the tooth substrate.

View Article: PubMed Central - PubMed

Affiliation: Biomaterials Science Research Unit, Faculty of Dentistry, University of Sydney, United Dental Hospital, NSW, Australia. luiz.bertassoni@sydney.edu.au

Show MeSH
Related in: MedlinePlus