{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T17:25:17Z","timestamp":1786987517232,"version":"build-2736575974"},"reference-count":39,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2026,6,24]],"date-time":"2026-06-24T00:00:00Z","timestamp":1782259200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"},{"start":{"date-parts":[[2026,6,24]],"date-time":"2026-06-24T00:00:00Z","timestamp":1782259200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100006087","name":"Direcci\u00f3n General de Asuntos del Personal Acad\u00e9mico, Universidad Nacional Aut\u00f3noma de M\u00e9xico","doi-asserted-by":"publisher","award":["IN213822"],"award-info":[{"award-number":["IN213822"]}],"id":[{"id":"10.13039\/501100006087","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Peptide Science"],"published-print":{"date-parts":[[2026,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>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\u2010rich surfaces. This study investigated the in\u00a0vitro effects of cementum attachment protein\u2010derived peptides, CAP\u2010pi and its phosphorylated analog CAP\u2010pip, 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\u2013calcium oxalate interactions. Both peptides altered crystal growth patterns and lattice organization in a concentration\u2010dependent manner. Peptide treatments induced marked morphological perturbations, promoted irregular and rosette\u2010like habits, and modified vibrational profiles. Furthermore, confocal microscopy revealed selective adsorption onto specific crystallographic regions, whereas molecular dynamics demonstrated enhanced peptide\u2013calcium coordination and interfacial stability for CAP\u2010pip. Collectively, these findings establish phosphorylation as a key determinant of peptide\u2013mineral interactions, providing mechanistic insight into how phosphopeptides regulate crystallization through surface\u2010mediated modulation.<\/jats:p>","DOI":"10.1002\/psc.70112","type":"journal-article","created":{"date-parts":[[2026,6,24]],"date-time":"2026-06-24T12:08:32Z","timestamp":1782302912000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Cementum Attachment Protein\u2010Derived Peptides Modulate Brushite and Calcium Oxalate Crystallization In\u00a0Vitro"],"prefix":"10.1002","volume":"32","author":[{"ORCID":"https:\/\/orcid.org\/0009-0005-0087-1150","authenticated-orcid":false,"given":"Alberto","family":"Mimila\u2010Cortes","sequence":"first","affiliation":[{"name":"Laboratorio de Biolog\u00eda Periodontal y Tejidos Mineralizados Universidad Nacional Aut\u00f3noma de M\u00e9xico  Mexico City 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