Nanomechanical characterization of time-dependent deformation/recovery on human dentin caused by radiation-induced glycation. (February 2019)

• Record Type: Journal Article
• Authors: Tobe, Takuma; Shibata, Yo; Mochizuki, Ayako; Shimomura, Naofumi; Zhou, Jun; Wurihan, ; Tanaka, Reina; Ikeda, Sachiko; Zhang, Zhongpu; Li, Qing; Inoue, Tomio; Miyazaki, Takashi
• Is Part Of: Journal of the mechanical behavior of biomedical materials. Volume 90(2019)
• Page Start: 248
• Page End: 255
• Publication Date: 2019-02
• Subjects: Mineralized tissue -- Dentin -- Advanced glycation end products -- Nanoindentation -- Raman; Biomedical materials -- Periodicals; Biomedical materials -- Mechanical properties -- Periodicals; Biomedical materials; Biomedical materials -- Mechanical properties; Periodicals; Electronic journals; 610.28
• DOI: 10.1016/j.jmbbm.2018.10.015
• Languages: English
• ISSNs: 1751-6161

Abstract

Abstract: An increase in non-enzymatic collagen matrix cross-links, such as advanced glycation end-products (AGEs), is known to be a major complication in human mineralized tissues, often causing abnormal fractures. However, degradation of mechanical properties in relation to AGEs has not been fully elucidated at the material level. Here, we report nanoscale time-dependent deformation and dimensional recovery of human tooth dentin that has undergone glycation induced by x-ray irradiation. The reduction in enzymatic collagen cross-linking and the increased level of AGEs with concomitant growth of disordered collagen matrix diminished creep deformation recovery in the lower mineralized target region. However, the elevated AGEs level alone did not cause a reduction in time-dependent deformation and its recovery in the higher mineralized target region. In addition to the elevated AGEs level, the degradation of the mechanical properties of mineralized tissues should be assessed with care in respect to multiple parameters in the collagen matrix at the molecular level. Graphical abstract: X-ray irradiation of human tooth dentin causes the matrix deterioration, including reduction in enzymatic collagen cross-linking with concomitant growth of AGEs and disordered collagen matrix.