ArticleBiomacromolecules2024
O-glycans Expand Lubricin and Attenuate Its Viscosity and Shear Thinning.
Article in Biomacromolecules, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Lubricin Levels in Temporomandibular Joint Disorders: A Scoping Review.International journal of molecular sciences · 2026Article
- A Coarse-Grained MARTINI Model for Mucins.Journal of chemical theory and computation · 2026Article
- Lubricin in osteoarthritis: functions and therapeutic prospects.Frontiers in immunology · 2026Review
- Lubricin's Mucin Domain Has Strong Polyproline Type II Helical Character.Computational and structural biotechnology journal · 2026Article
- Lectin Microarray-based Glycomics and Machine Learning Identify Shared Osteoarthritis Biomarkers in Humans, Dogs, and Horses.bioRxiv : the preprint server for biology · 2025Article
- Refined Protein-Sugar Interactions in the Martini Force Field.Journal of chemical theory and computation · 2024Article
- Breaking Down the Bottlebrush: Atomically Detailed Structural Dynamics of Mucins.Journal of chemical information and modeling · 2024Article
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Authors and funding
7 authors.
Funding
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Abstract
Lubricin, an intrinsically disordered glycoprotein, plays a pivotal role in facilitating smooth movement and ensuring the enduring functionality of synovial joints. The central domain of this protein serves as a source of this excellent lubrication and is characterized by its highly glycosylated, negatively charged, and disordered structure. However, the influence of O-glycans on the viscosity of lubricin remains unclear. In this study, we employ molecular dynamics simulations in the absence and presence of shear, along with continuum simulations, to elucidate the intricate interplay between O-glycans and lubricin and the impact of O-glycans on lubricin's conformational properties and viscosity. We found the presence of O-glycans to induce a more extended conformation in fragments of the disordered region of lubricin. These O-glycans contribute to a reduction in solution viscosity but at the same time weaken shear thinning at high shear rates, compared to nonglycosylated systems with the same density. This effect is attributed to the steric and electrostatic repulsion between the fragments, which prevents their conglomeration and structuring. Our computational study yields a mechanistic mechanism underlying previous experimental observations of lubricin and paves the way to a more rational understanding of its function in the synovial fluid.
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Registered trials
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