Biomolecular Origin of The Rate-Dependent Deformation of Prismatic Enamel

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Penetration deformation of columnar prismatic enamel was investigated using instrumented nanoindentation testing, carried out at three constant strain rates (0.05 s{sup -1}, 0.005 s{sup -1}, and 0.0005 s{sup -1}). Enamel demonstrated better resistance to penetration deformation and greater elastic modulus values were measured at higher strain rates. The origin of the rate-dependent deformation was rationalized to be the shear deformation of nanoscale protein matrix surrounding each hydroxyapatite crystal rods. And the shear modulus of protein matrix was shown to depend on strain rate in a format: G{sub p} = 0.213 + 0.021 ln {dot {var_epsilon}}. Most biological composites compromise reinforcement ... continued below

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12 p. (0.2 MB)

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Zhou, J & Hsiung, L July 5, 2006.

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Penetration deformation of columnar prismatic enamel was investigated using instrumented nanoindentation testing, carried out at three constant strain rates (0.05 s{sup -1}, 0.005 s{sup -1}, and 0.0005 s{sup -1}). Enamel demonstrated better resistance to penetration deformation and greater elastic modulus values were measured at higher strain rates. The origin of the rate-dependent deformation was rationalized to be the shear deformation of nanoscale protein matrix surrounding each hydroxyapatite crystal rods. And the shear modulus of protein matrix was shown to depend on strain rate in a format: G{sub p} = 0.213 + 0.021 ln {dot {var_epsilon}}. Most biological composites compromise reinforcement mineral components and an organic matrix. They are generally partitioned into multi-level to form hierarchical structures that have supreme resistance to crack growth [1]. The molecular mechanistic origin of toughness is associated with the 'sacrificial chains' between the individual sub-domains in a protein molecule [2]. As the protein molecule is stretched, these 'sacrificial chains' break to protect its backbone and dissipate energy [3]. Such fresh insights are providing new momentum toward updating our understanding of biological materials [4]. Prismatic enamel in teeth is one such material. Prismatic microstructure is frequently observed in the surface layers of many biological materials, as exemplified in mollusk shells [5] and teeth [6]. It is a naturally optimized microstructure to bear impact loading and penetration deformation. In teeth, the columnar prismatic enamel provides mechanical and chemical protection for the relatively soft dentin layer. Its mechanical behavior and reliability are extremely important to ensure normal tooth function and human health. Since enamel generally contains up to 95% hydroxyapatite (HAP) crystals and less than 5% protein matrix, it is commonly believed to be a weak and brittle material with little resistance to fracture [7]. This study is aimed at exploring the effect of the weak amelogenin-rich protein matrix on the overall mechanical behavior of prismatic enamel. The experimental work involves applying contact loads at various strain rates to carefully prepared enamel specimens using an instrumented nanoindentater. The enamel material and specimen preparation procedure were described in a previous study [8]. Briefly, the enamel was dissected into small blocks about 2 mm wide and 1 mm thick. These small blocks had relatively flat surfaces, under which the prisms were uniformly perpendicular to the top surfaces for nanoindentation testing [9,10]. The small blocks were then embedded, ground, and finishing polished with 0.03 {micro}m diamond suspension. Nanoindentation testing was carried out in a MTS XP{reg_sign} nanoindenter (MTS nano instrument, Oak Ridge, TN). Each test consisted of three segments, including a loading process, a holding period at the maximum load for a certain time, and a final unloading process. The loading process was carried out under constant strain rbate [11] to reach a defined penetration depth, corresponding to which the maximum load was reached.

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12 p. (0.2 MB)

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PDF-file: 12 pages; size: 0.2 Mbytes

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  • Journal Name: Applied Physics Letters, vol. 89, no. 5, July 31, 2006, pp. 051904

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  • Report No.: UCRL-JRNL-222701
  • Grant Number: W-7405-ENG-48
  • Office of Scientific & Technical Information Report Number: 894752
  • Archival Resource Key: ark:/67531/metadc887146

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  • July 5, 2006

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  • Sept. 22, 2016, 2:13 a.m.

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  • April 13, 2017, 3:58 p.m.

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Zhou, J & Hsiung, L. Biomolecular Origin of The Rate-Dependent Deformation of Prismatic Enamel, article, July 5, 2006; Livermore, California. (digital.library.unt.edu/ark:/67531/metadc887146/: accessed December 11, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.