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Original Article
The effect of ethylene glycol analogs on mechanical properties of moist demineralized dentin matrix
Kyung-Ha Lee, Young-Gon Cho, Kwang-Won Lee
J Korean Acad Conserv Dent 2006;31(4):290-299.   Published online July 31, 2006
DOI: https://doi.org/10.5395/JKACD.2006.31.4.290
AbstractAbstract PDFPubReaderePub
Objectives

The purpose of this study is to evaluate the effect of ethylene glycol analogs on modulus of elasticity and ultimate tensile strength of moist, demineralized dentin matrix.

Methods

Dentin disks 0.5 mm thick were prepared from mid-coronal dentin of extracted, unerupted, human third molars. "I" beam and hour-glass shaped specimens were prepared from the disks, the ends protected with nail varnish and the central regions completely demineralized in 0.5M EDTA for 5 days. Ultimate tensile stress (UTS) and low strain modulus of elasticity (E) were determined with specimens immersed for 60 min in distilled water (H2O), ethylene glycol (HO-CH2-CH2-OH), 2-methoxyethanol (H3CO-CH2-CH2-OH), and 1,2-dimethoxyethane (H3CO-CH2-CH3-OCH3) prior to testing in those same media. Modulus of elasticity was measured on the same specimens in a repeated measures experimental design. The results were analyzed with a one-way ANOVA on ranks, followed by Dunn's test at α = 0.05. Regression analysis examined the relationship between UTS or E and hoy's solubility parameter for hydrogen bonding (δh) of each solvent.

Results

The UTS of demineralized dentin in water, ethylene glycol, 2-methoxyethanol, and 1,2-dimethoxyethane was 24 (3), 30 (5), 37 (6), and 45 (6) MPa, × (SD) N = 10. Low strain E for the same media were 16 (13), 23 (14), 52 (24), and 62 (22) MPa. Regression analysis of UTS vs δh revealed a significant (p < 0.0001, r = -0.99, R2 = 0.98) inverse, exponential relationship. A similar inverse relationship was obtained between low strain E vs δh (p < 0.0005, r = -0.93, R2 = 0.86).

Significance

The tensile properties of demineralized dentin are dependent upon the hydrogen bonding ability of polar solvents (δh). Solvents with low δh values may permit new interpeptide H-bonding in collagen that increases its tensile properties. Solvents with high δh values prevent the development of these new interpeptide H-bonds.

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