Cross-linked demineralized dentin maintains its mechanical stability when challenged by bacterial collagenase.
Cross-linked demineralized dentin maintains its mechanical stability when challenged by bacterial collagenase.
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DOI:
10.1002/jbm.b.31759
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发表时间:
2011-02
影响因子:
3.4
通讯作者:
Wang, Yong
中科院分区:
文献类型:
--
作者:
Xu, Changqi;Wang, Yong
The molecular structure, weight loss and mechanical properties of demineralized dentin of non-crosslinked/crosslinked by glutaraldehyde (GA) were investigated when being challenged by bacterial collagenase solution over time in the present study. Raman spectra proved that cross-linking occurred in demineralized dentin matrices after being treated with GA. Meanwhile, the weight of the cross-linked demineralized dentin matrices didn’t change after being challenged by bacterial collagenase solution up to one week. However, the weight of non-crosslinked dentin collagen fell by almost 45% after degradation for 5 hr, and up to 100% after 19 hr. The tensile strength of demineralized dentin matrices didn’t show a significant change after being crosslinked, while the stiffness of demineralized dentin matrices showed more improvement than that of non-crosslinked collagen. The toughness of demineralized dentin matrices decreased slightly after being crosslinked. Importantly, neither the tensile strength of GA-crosslinked demineralized dentin nor its stiffness changed over time in either control buffer or collagenase solution compared to that of noncrosslinked controls. These results suggested that improving the degree of cross-linking in dentin collagen could be one method to inhibit its biodegradation and further to increase the durability of dental restorations.
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DOI:
10.1002/jmb.b.31022
发表时间:
2008-08-01
影响因子:
3.4
作者:
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通讯作者:
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DOI:
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发表时间:
2003-01-01
影响因子:
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DOI:
10.1016/s0169-7439(98)00084-7
发表时间:
1998-09-28
影响因子:
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作者:
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通讯作者:
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影响因子:
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