{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,25]],"date-time":"2026-04-25T15:03:47Z","timestamp":1777129427240,"version":"3.51.4"},"reference-count":43,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2015,6,17]],"date-time":"2015-06-17T00:00:00Z","timestamp":1434499200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Grant-in-Aid for Scientific Research from the Japan Society for the Promotion of Science.","award":["25462949"],"award-info":[{"award-number":["25462949"]}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["European J Oral Sciences"],"published-print":{"date-parts":[[2015,8]]},"abstract":"<jats:p>Salivary phosphoproteins are essential in tooth mineral regulation but are often overlooked in\u00a0vitro. This study aimed to evaluate the effect of casein, as a salivary phosphoprotein homologue, on the deposition and growth of hydroxyapatite (HA) on tooth surfaces. Hydroxyapatite growth was quantified using seeded crystal systems. Artificial saliva (<jats:styled-content style=\"fixed-case\">AS<\/jats:styled-content>) containing <jats:styled-content style=\"fixed-case\">HA<\/jats:styled-content> powder and 0, 10, 20, 50, or 100\u00a0<jats:italic>\u03bc<\/jats:italic>g\u00a0ml<jats:sup>\u22121<\/jats:sup> of casein, or 100\u00a0<jats:italic>\u03bc<\/jats:italic>g\u00a0ml<jats:sup>\u22121<\/jats:sup> of dephosphorylated casein (Dcasein), was incubated for 0\u20138\u00a0h at 37\u00b0C, <jats:styled-content style=\"fixed-case\">pH<\/jats:styled-content> 7.2. Calcium concentrations were measured using atomic absorption spectroscopy (<jats:styled-content style=\"fixed-case\">AAS<\/jats:styled-content>). Surface precipitation of <jats:styled-content style=\"fixed-case\">HA<\/jats:styled-content> on bovine enamel and dentine blocks, incubated in similar conditions for 7\u00a0d, was examined using field emission scanning electron microscopy (<jats:styled-content style=\"fixed-case\">FE<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">SEM<\/jats:styled-content>) and transmission electron microscopy (<jats:styled-content style=\"fixed-case\">TEM<\/jats:styled-content>) with selected area electron diffraction (<jats:styled-content style=\"fixed-case\">SAED<\/jats:styled-content>). Casein adsorption was assessed using modified Lowry assays and zeta\u2010potential measurements. The <jats:styled-content style=\"fixed-case\">AAS<\/jats:styled-content> results revealed a concentration\u2010dependent inhibition of calcium consumption. Hydroxyapatite precipitation occurred when no casein was present, whereas precipitation of <jats:styled-content style=\"fixed-case\">HA<\/jats:styled-content> was apparently completely inhibited in casein\u2010containing groups. Adsorption data demonstrated increasingly negative zeta\u2010potential with increased casein concentration and an affinity constant similar to proline\u2010rich proteins with Langmuir modelling. Casein inhibited the deposition and growth of <jats:styled-content style=\"fixed-case\">HA<\/jats:styled-content> primarily through the binding of esterized phosphate to <jats:styled-content style=\"fixed-case\">HA<\/jats:styled-content> active sites, indicating its potential as a mineral\u2010regulating salivary phosphoprotein homologue in\u00a0vitro.<\/jats:p>","DOI":"10.1111\/eos.12196","type":"journal-article","created":{"date-parts":[[2015,6,17]],"date-time":"2015-06-17T13:09:23Z","timestamp":1434546563000},"page":"288-296","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Inhibition of hydroxyapatite growth by casein, a potential salivary phosphoprotein homologue"],"prefix":"10.1111","volume":"123","author":[{"given":"Maria J. R. 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