ArticleMatrix biology : journal of the International Society for Matrix Biology2015
Preferential sites for intramolecular glucosepane cross-link formation in type I collagen: A thermodynamic study.
Article in Matrix biology : journal of the International Society for Matrix Biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Sites of non-enzymatic crosslinks pentosidine and glucosepane in collagen I of human cortical bone.Bone · 2026Article
- Mineral and cross-linking in collagen fibrils: The mechanical behavior of bone tissue at the nano-scale.Journal of the mechanical behavior of biomedical materials · 2024Article
- An overview on glycation: molecular mechanisms, impact on proteins, pathogenesis, and inhibition.Biophysical reviews · 2024Review
- Advanced-Glycation Endproducts: How cross-linking properties affect the collagen fibril behavior.Journal of the mechanical behavior of biomedical materials · 2023Article
- Impaired angiogenesis in ageing: the central role of the extracellular matrix.Journal of translational medicine · 2023Review
- Article
- Contrasting Local and Macroscopic Effects of Collagen Hydroxylation.International journal of molecular sciences · 2021Article
- Lysine-arginine advanced glycation end-product cross-links and the effect on collagen structure: A molecular dynamics study.Proteins · 2021Article
- Collagen Biosynthesis, Processing, and Maturation in Lung Ageing.Frontiers in medicine · 2021Review
- Generation and Characterization of Anti-Glucosepane Antibodies Enabling Direct Detection of Glucosepane in Retinal Tissue.ACS chemical biology · 2020Article
- Allosteric Communications between Domains Modulate the Activity of Matrix Metalloprotease-1.Biophysical journal · 2020Article
- Glycation of type I collagen selectively targets the same helical domain lysine sites as lysyl oxidase-mediated cross-linking.The Journal of biological chemistry · 2018Article
- Effect on the mechanical properties of type I collagen of intra-molecular lysine-arginine derived advanced glycation end-product cross-linking.Journal of biomechanics · 2018Article
- Combining nano-physical and computational investigations to understand the nature of "aging" in dermal collagen.International journal of nanomedicine · 2017Article
- Intra-molecular lysine-arginine derived advanced glycation end-product cross-linking in Type I collagen: A molecular dynamics simulation study.Biophysical chemistry · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The extracellular matrix (ECM) undergoes progressive age-related stiffening and loss of proteolytic digestibility due to an increase in concentration of advanced glycation end products (AGEs). The most abundant AGE, glucosepane, accumulates in collagen with concentrations over 100 times greater than all other AGEs. Detrimental collagen stiffening properties are believed to play a significant role in several age-related diseases such as osteoporosis and cardiovascular disease. Currently little is known of the potential location of covalently cross-linked glucosepane formation within collagen molecules; neither are there reports on how the respective cross-link sites affect the physical and biochemical properties of collagen. Using fully atomistic molecular dynamics simulations (MD) we have identified six sites where the formation of a covalent intra-molecular glucosepane cross-link within a single collagen molecule in a fibrillar environment is energetically favourable. Identification of these favourable sites enables us to align collagen cross-linking with experimentally observed changes to the ECM. For example, formation of glucosepane was found to be energetically favourable within close proximity of the Matrix Metalloproteinase-1 (MMP1) binding site, which could potentially disrupt collagen degradation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.