ArticleJournal of peptide science : an official publication of the European Peptide Society2026
Cementum Attachment Protein-Derived Peptides Modulate Brushite and Calcium Oxalate Crystallization In Vitro.
Article in Journal of peptide science : an official publication of the European Peptide Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Cementum Attachment Protein-Derived Peptides Modulate Brushite and Calcium Oxalate Crystallization In Vitro.Journal of peptide science : an official publication of the European Peptide Society · 2026Article
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Authors and funding
10 authors.
Funding
Abstract
Pathological mineralization involves the uncontrolled crystallization of calcium phosphate (brushite) and calcium oxalate, leading to renal calculi and ectopic calcifications. Peptides enriched in acidic or phosphorylated residues are potential crystal growth modulators due to their ability to interact with calcium-rich surfaces. This study investigated the in vitro effects of cementum attachment protein-derived peptides, CAP-pi and its phosphorylated analog CAP-pip, on brushite and calcium oxalate crystallization. By isolating these highly anionic motifs, this work introduces a novel biomimetic approach to investigate and modulate the physicochemical mechanisms driving pathological mineral deposition. Assays performed under physiological conditions were analyzed by scanning electron microscopy, Raman spectroscopy, and confocal microscopy, alongside molecular dynamics simulations to examine peptide-calcium oxalate interactions. Both peptides altered crystal growth patterns and lattice organization in a concentration-dependent manner. Peptide treatments induced marked morphological perturbations, promoted irregular and rosette-like habits, and modified vibrational profiles. Furthermore, confocal microscopy revealed selective adsorption onto specific crystallographic regions, whereas molecular dynamics demonstrated enhanced peptide-calcium coordination and interfacial stability for CAP-pip. Collectively, these findings establish phosphorylation as a key determinant of peptide-mineral interactions, providing mechanistic insight into how phosphopeptides regulate crystallization through surface-mediated modulation.
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