Effect on the mechanical properties of type I collagen of intra-molecular lysine-arginine derived advanced glycation end-product cross-linking.

Effect on the mechanical properties of type I collagen of intra-molecular lysine-arginine derived advanced glycation end-product cross-linking.
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对分子内赖氨酸 - 精氨酸衍生的晚期糖基化最终产物交联的I型胶原蛋白的机械性能的影响。

DOI:
10.1016/j.jbiomech.2017.11.021
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发表时间:
2018-01-23
影响因子:
2.4
通讯作者:
de Leeuw NH
de Leeuw NH
中科院分区:
工程技术3区
文献类型:
--
作者:
Collier TA;Nash A;Birch HL;de Leeuw NH

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胶原分子的非酶晚期糖基化终末产物(AGE)交联会导致体内结缔组织的机械性能发生显著变化,可能导致许多与AGE相关的疾病。我们用分子动力学的方法研究了两种交联剂,葡糖胺和DOGDIC对胶原蛋白分子的拉伸和侧向模数的影响,利用分子内交联剂的优先形成位置。结果表明,分子内年龄交联剂的存在使低应变区的拉伸和侧向杨氏模数分别提高了3.0-8.5%和2.9-60.3%,而在高应变区几乎没有影响。
Non-enzymatic advanced glycation end product (AGE) cross-linking of collagen molecules has been hypothesised to result in significant changes to the mechanical properties of the connective tissues within the body, potentially resulting in a number of age related diseases. We have investigated the effect of two of these cross-links, glucosepane and DOGDIC, on the tensile and lateral moduli of the collagen molecule through the use of a steered molecular dynamics approach, using previously identified preferential formation sites for intra-molecular cross-links. Our results show that the presence of intra-molecular AGE cross-links increases the tensile and lateral Young’s moduli in the low strain domain by between 3.0–8.5% and 2.9–60.3% respectively, with little effect exhibited at higher strains.
DOI: 10.1557/jmr.2006.0236
发表时间: 2006-08-01
影响因子: 2.7
作者:
Buehler, Markus J.
通讯作者: Buehler, Markus J.
DOI: 10.1196/annals.1333.061
发表时间: 2005-01-01
期刊: MAILLARD REACTION: CHEMISTRY AT THE INTERFACE OF NUTRITION, AGING, AND DISEASE
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期刊: Matrix biology : journal of the International Society for Matrix Biology
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作者:
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通讯作者: de Leeuw NH
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发表时间: 2002-07-12
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