The Effects of Alcoholic Compounds on the Type I Collagen Studied by Differential Scanning Stability of Calorimetry.

Fukuda, Kyosuke; Noji, Takashi; Terada, Yoshihiro

doi:10.4012/dmj.19.221

Cited by 13 publications

(21 citation statements)

References 11 publications

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“…Such dehydration of demineralized dentin by air-drying increases the packing density of collagen molecules and produces loss of volume due to surface tension forces 23) . However, dehydration in organic solvents prevented exposure of collagen molecules to the surface tension forces in air, stiffened the interfibrillar spaces with less shrinkage, and improved preservation of the spaces when subsequently exposed to air 17,18,22) . Both air-drying and dehydration in organic solvents may serve to stiffen demineralized dentin matrix, but their effect on the volume change of the collagen structure differed 17) .…”

Section: ⅳ Discussionmentioning

confidence: 99%

“…This finding suggests that solvent-priming on etched wet dentin might effectively replace water to solvents, stabilize the three dimensional structure of collagen network, and facilitate penetration of the experimental adhesives into the collagen networks floating in the solvent. After etching and rinsing procedures, water molecules bind to the carbonyl groups protruding from collagen helices, forming hydrogen bonds and serving to stabilize the ordered triple helix structure 18,22) . When exposed collagen structure is dried abruptly, loss of unbound water may stabilize the collagen fibrillar structure by increasing the interaction between adjacent collagen molecules.…”

Section: ⅳ Discussionmentioning

confidence: 99%

“…An aqueous solution of HEMA applied to the dentin improved the substrate' s penetrability, substantiated apparent hybrid layer, and improved bond strength, when the dentin was pretreated with an aqueous solution of 10% citric acid and 3% ferric chloride, rinsed with water and air-dried 19) . Like HEMA, alcohols at higher concentration also significantly stabilized collagen 18) . High vapor pressure solvents such as acetone and ethanol have been used to compete with and displace water and to facilitate the permeation of monomers 20) .…”

Section: ⅰ Introductionmentioning

confidence: 99%

“…High vapor pressure solvents such as acetone and ethanol have been used to compete with and displace water and to facilitate the permeation of monomers 20) . Although hydrophobic bisphenol-A-glycidylmethacrylate (Bis-GMA) and triethyleneglycol dimethacrylate (TEGDMA) are not chemically compatible with wet dentin 2) , the chain length-dependent surface tension of alcohols may affect the stability of collagen and control the permeation of the adhesives through the fibers 18) . In order to increase the durability of dentin adhesives, by priming the collagen network exposed after etching and rinsing procedures with organic solvents, we tried to remove water from the collagen network without collapse.…”

Section: ⅰ Introductionmentioning

confidence: 99%

“…In order to improve the durability of dentin adhesives, there may be two approaches for reducing hydrophilic domains; complete removal of water from the exposed collagen network without deteriorating the integrity of its threedimensional structure and substitution of hydrophilic monomers in the adhesives with more hydrophobic monomers which can resist hydrolysis. Some organic substances and solvents including HEMA and monohydric alcohols are known to stiffen collagen 17,18) . An aqueous solution of HEMA applied to the dentin improved the substrate' s penetrability, substantiated apparent hybrid layer, and improved bond strength, when the dentin was pretreated with an aqueous solution of 10% citric acid and 3% ferric chloride, rinsed with water and air-dried 19) .…”

Section: ⅰ Introductionmentioning

confidence: 99%

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The effect of priming etched dentin with solvent on the microtensile bond strength of hydrophobic dentin adhesive

Park

Bae

Kim

et al. 2009

J Korean Acad Conserv Dent

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Deterioration of long-term dentin adhesion durability is thought to occur by hydrolytic degradation within hydrophilic domains of the adhesive and hybrid layers. This study investigated the hypothesis that priming the collagen network with an organic solvent displace water without collapse and thereby obtain good bond strength with an adhesive made of hydrophobic monomers and organic solvents. Three experimental adhesives were prepared by dissolving two hydrophobic monomers, bisphenol-A-glycidylmethacrylate (Bis-GMA) and triethyleneglycol dimethacrylate (TEGDMA), into acetone, ethanol or methanol. After an etching and rinsing procedure, the adhesives were applied onto either wet dentin surfaces (wet bonding) or dentin surfaces primed with the same solvent (solvent-primed bonding). Microtensile bond strength (MTBS) was measured at 48 hrs, 1 month and after 10,000 times of thermocycles. The bonded interfaces were evaluated using a scanning electron microscope (SEM). Regardless of bonding protocols, well-developed hybrid layers were observed at the bonded interface in most specimens. The highest mean MTBS was observed in the adhesive containing ethanol at 48 hrs. With solvent-primed bonding, increased MTBS tendencies were seen with thermocycling in the adhesives containing ethanol or methanol. However, in the case of wet bonding, no increase in MTBS was observed with aging. Ⅰ. IntroductionThe bonding mechanism of dentin adhesives currently available is partly based on the micromechanical retention through formation of a hybrid layer 1) . In order to obtain consistent hybrid layers, the threedimensional structure of a collagen network should be exposed by etchant or acidic monomers. Water is required to obtain the appropriate acidity of etchants or acidic monomers. During infiltration of resin monomers, the interfibrillar space of the collagen network should be maintained by being floated in water. Therefore, as an essential component, hydrophilic monomers are incorporated into adhesives applied on dentin. From the view point of 'long-term durability' , the bonding procedure itself involves several inherent risk factors. These factors include collagen fibers denatured by strong acid, water used to float the collagen network, phase separation between the hydrophilic and hydrophobic monomers, and the resulting exposure of hydrophilic resin monomers and collagens which are weak to hydrolytic attack.During wet bonding, the hydrophobic and hydrophilic monomers dissolved in solvents such as ABSTRACT *Corresponding

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Section: ⅳ Discussionmentioning

confidence: 99%

Section: ⅳ Discussionmentioning

confidence: 99%

Section: ⅰ Introductionmentioning

confidence: 99%

Section: ⅰ Introductionmentioning

confidence: 99%

Section: ⅰ Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The effect of priming etched dentin with solvent on the microtensile bond strength of hydrophobic dentin adhesive

Park

Bae

Kim

et al. 2009

J Korean Acad Conserv Dent

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Region‐specific role of water in collagen unwinding and assembly

Ravikumar

Hwang

2008

Proteins

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Conformational stability of the collagen triple helix affects its turnover and determines tissue homeostasis. Although it is known that the presence of imino acids (prolines or hydroxyprolines) confer stability to the molecule, little is known regarding the stability of the imino-poor region lacking imino acids, which plays a key role in collagen cleavage. In particular, there have been continuing debates about the role of water in collagen stability. We addressed these issues using molecular dynamics simulations on 30-residue long collagen triple helices, including a structure that has a biologically relevant 9-residue imino-poor region from type III collagen (PDB ID: 1BKV). A torsional map approach was used to characterize the conformational motion of the molecule that differ between imino-rich and imino-poor regions. At temperatures 300 K and above, unwinding initiates at a common cleavage site, the glycine-isoleucine bond in the imino-poor region. This provides a linkage between previous observations that unwinding of the imino-poor region is a requirement for collagenase cleavage, and that isolated collagen molecules are unstable at body temperature. We found that unwinding of the imino-poor region is controlled by dynamic water bridges between backbone atoms with average lifetimes on the order of a few picoseconds, as the degree of unwinding strongly correlated with the loss of water bridges, and unwinding could be either prevented or enhanced, respectively by enforcing or forbidding water bridge formation. While individual water bridges were short-lived in the imino-poor region, the hydration shell surrounding the entire molecule was stable even at 330 K. The diameter of the hydrated collagen including the first hydration shell was about 14 A, in good agreement with the experimentally measured inter-collagen distances. These results elucidate the general role of water in collagen turnover: water not only affects collagen cleavage by controlling its torsional motion, but it also forms a larger-scale lubrication layer mediating collagen self-assembly.

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