ArticleUrolithiasis2019
Incorporation of osteopontin peptide into kidney stone-related calcium oxalate monohydrate crystals: a quantitative study.
Article in Urolithiasis, 2019. 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, 15 citations in OpenAlex.
- Intercalated bacterial biofilms are intrinsic internal components of calcium-based kidney stones.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Multi - dimensional mechanism analysis ofFrontiers in pharmacology · 2025Article
- Characteristics of kidney stone-modulatory proteins decoded from proteins identified in stone matrix and urine of stone formers and non-stone subjects.Computational and structural biotechnology journal · 2025Article
- Annexin-derived self-assembling peptide nanostructures for alleviation of calcium oxalate -induced renal injury.Urolithiasis · 2024Article
- Osteopontin phosphopeptide mitigates calcium oxalate stone formation in a Drosophila melanogaster model.Urolithiasis · 2022Article
- Multicolor imaging of calcium-binding proteins in human kidney stones for elucidating the effects of proteins on crystal growth.Scientific reports · 2021Article
- Idiopathic Osteoporosis and Nephrolithiasis: Two Sides of the Same Coin?International journal of molecular sciences · 2020Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Polyelectrolyte-crystal interactions regulate many aspects of biomineralization, including the shape, phase, and aggregation of crystals. Here, we quantitatively investigate the role of phosphorylation in interactions with calcium oxalate monohydrate crystals (COM), using synthetic peptides corresponding to the sequence 220-235 in osteopontin, a major inhibitor of kidney stone-related COM formation. COM formation is induced in the absence or presence of fluorescent-labeled peptides containing either no (P0), one (P1) or three (P3) phosphates and their adsorption to and incorporation into crystals determined using quantitative fluorimetry (also to determine maximum adsorption/incorporation), confocal/scanning electron microscopy and X-ray/Raman spectroscopy. Results demonstrate that higher phosphorylated peptides show stronger irreversible adsorption to COM crystals (P3: K
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