Preferential sites for intramolecular glucosepane cross-link formation in type I collagen: A thermodynamic study
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- 作者：Thomas A. Collier1 ; t.collier.12@ucl.ac.uk" class="auth_mail" title="E-mail the corresponding author ; Anthony Nash1 ; Helen L. Birch2 ; Nora H. de Leeuw1
- 关键词：ECM ; extracellular matrix ; MD ; molecular dynamics ; AGEs ; advanced glycation end products ; SLRP ; small leucine-rich proteoglycan ; HS ; heparan sulphate ; HSP-47 ; heat shock protein 47 ; MMP1 ; Matrix Metalloproteinase-1 ; DS ; dermatan sulphate ; MIDAS ; metal ion-dependent adhesion site ; IL-2 ; interleukin 2
- 刊名：Matrix Biology
- 出版年：2015
- 出版时间：October 2015
- 年：2015
- 卷：48
- 期：Complete
- 页码：78-88
- 全文大小：979 K
文摘
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We conduct fully atomistic molecular dynamics simulation of fibrillar collagen.
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Glucosepane cross-link formation is energetically favourable at six positions.
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Positions identified are within key collagen biomolecule sites.
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Positioning of sites may have a significant effect on tissue function and integrity.