ArticleProteins2021
Lysine-arginine advanced glycation end-product cross-links and the effect on collagen structure: A molecular dynamics study.
Article in Proteins, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Three Water Molecules Mediate Ring Opening of d‑Glucose in Aqueous Solutions.ACS physical chemistry Au · 2026Article
- Alterations in hepatic amino acid metabolism related to MASLD in individuals with obesity.Journal of physiology and biochemistry · 2025Article
- The role of oxidative post-translational modifications in type 1 diabetes pathogenesis.Frontiers in immunology · 2025Review
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Integrated 4D label-free proteomics and data mining to elucidate the effects of thermal processing on crisp grass carp protein profiles.Current research in food science · 2024Article
- The influence of AGEs and enzymatic cross-links on the mechanical properties of collagen fibrils.Journal of the mechanical behavior of biomedical materials · 2023Article
- Regulators of collagen crosslinking in developing and adult tendons.European cells & materials · 2022Review
- Lysine-arginine advanced glycation end-product cross-links and the effect on collagen structure: A molecular dynamics study.Proteins · 2021Article
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 1 country.
Funding
Abstract
The accumulation of advanced glycation end-products is a fundamental process that is central to age-related decline in musculoskeletal tissues and locomotor system function and other collagen-rich tissues. However, although computational studies of advanced glycation end-product cross-links could be immensely valuable, this area remains largely unexplored given the limited availability of structural parameters for the derivation of force fields for Molecular Dynamics simulations. In this article, we present the bonded force constants, atomic partial charges and geometry of the arginine-lysine cross-links DOGDIC, GODIC, and MODIC. We have performed in vacuo Molecular Dynamics simulations to validate their implementation against quantum mechanical frequency calculations. A DOGDIC advanced glycation end-product cross-link was then inserted into a model collagen fibril to explore structural changes of collagen and dynamics in interstitial water. Unlike our previous studies of glucosepane, our findings suggest that intra-collagen DOGDIC cross-links furthers intra-collagen peptide hydrogen-bonding and does not promote the diffusion of water through the collagen triple helices.
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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.