ArticleJournal of the Royal Society, Interface2015
Dynamic footprint of sequestration in the molecular fluctuations of osteopontin.
Article in Journal of the Royal Society, Interface, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Functional Implications of Dynamic Structures of Intrinsically Disordered Proteins Revealed by High-Speed AFM Imaging.Biomolecules · 2022Review
- Hyperphosphorylation of Human Osteopontin and Its Impact on Structural Dynamics and Molecular Recognition.Biochemistry · 2021Article
- Mmu_circ_003795 regulates osteoblast differentiation and mineralization in MC3T3‑E1 and MDPC23 by targeting COL15A1.Molecular medicine reports · 2020Article
- A Novel 3D Osteoblast and Osteocyte Model Revealing Changes in Mineralization and Pro-osteoclastogenic Paracrine Signaling During Estrogen Deficiency.Frontiers in bioengineering and biotechnology · 2020Article
- Dynamical Oligomerisation of Histidine Rich Intrinsically Disordered ProteinS Is Regulated through Zinc-Histidine Interactions.Biomolecules · 2019Article
- A quantitative model of the bovine casein micelle: ion equilibria and calcium phosphate sequestration by individual caseins in bovine milk.European biophysics journal : EBJ · 2019Article
- Effect of Phosphorylation on a Human-like Osteopontin Peptide.Biophysical journal · 2017Article
- Intrinsically disordered proteins and biomineralization.Matrix biology : journal of the International Society for Matrix BiologyReview
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sequestration of calcium phosphate by unfolded proteins is fundamental to the stabilization of biofluids supersaturated with respect to hydroxyapatite, such as milk, blood or urine. The unfolded state of osteopontin (OPN) is thought to be a prerequisite for this activity, which leads to the formation of core-shell calcium phosphate nanoclusters. We report on the structures and dynamics of a native OPN peptide from bovine milk, studied by neutron spectroscopy and small-angle X-ray and neutron scattering. The effects of sequestration are quantified on the nanosecond- ångström resolution by elastic incoherent neutron scattering. The molecular fluctuations of the free phosphopeptide are in agreement with a highly flexible protein. An increased resilience to diffusive motions of OPN is corroborated by molecular fluctuations similar to those observed for globular proteins, yet retaining conformational flexibilities. The results bring insight into the modulation of the activity of OPN and phosphopeptides with a role in the control of biomineralization. The quantification of such effects provides an important handle for the future design of new peptides based on the dynamics-activity relationship.
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