ArticleChembiochem : a European journal of chemical biology2021
Binding Mode Characterization of Osteopontin on Hydroxyapatite by Solution NMR Spectroscopy.
Article in Chembiochem : a European journal of chemical biology, 2021. 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, 10 citations in OpenAlex.
- Article
- Article
- Deep Learning for Hyperpolarized NMR of Intrinsically Disordered Proteins without Resolution Loss: Access to Short-Lived Intermediates.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- The impact of hydroxyapatite crystal structures and protein interactions on bone's mechanical properties.Scientific reports · 2024Article
- Review
- How phosphorylation impacts intrinsically disordered proteins and their function.Essays in biochemistry · 2022Article
- Binding Mode Characterization of Osteopontin on Hydroxyapatite by Solution NMR Spectroscopy.Chembiochem : a European journal of chemical biology · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Extracellular matrix glycoproteins play a major role in bone mineralization and modulation of osteogenesis. Among these, the intrinsically disordered protein osteopontin (OPN) is associated with the inhibition of formation, growth and proliferation of the bone mineral hydroxyapatite (HAP). Furthermore, post-translational modifications like phosphorylation can alter conformations and interaction properties of intrinsically disordered proteins (IDPs). Therefore, the actual interaction of OPN with a HAP surface on an atomic level and how this interaction is affected by phosphorylation is of great interest. Here, we study the interaction of full-length OPN on the surface of suspended HAP nanoparticles by solution NMR spectroscopy. We report the binding modes of this IDP and provide evidence for the influence of hyperphosphorylation on the binding character and an explanation for the differing roles in biomineralization. Our study moreover presents an easy and suitable option to measure interaction of nanoparticles in a stable suspension with full-length proteins.
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Registered trials
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