Solution NMR structure of cementum protein 1 derived peptide (CEMP1-p1) and its role in the mineralization process.

Autor: Campos MN; Laboratorio de Biología Periodontal, Facultad de Odontología, Universidad Nacional Autónoma de México, Mexico City, Mexico., Giraldo EL; Chemistry Department, University of Colorado Denver, Denver, CO, USA., Del Rio Portilla F; Instituto de Química, Universidad Nacional Autónoma de México, Mexico City, Mexico., Fernández-Velasco DA; Facultad de Medicina, Universidad Nacional Autónoma de México, Mexico City, Mexico., Arzate H; Laboratorio de Biología Periodontal, Facultad de Odontología, Universidad Nacional Autónoma de México, Mexico City, Mexico., Romo-Arévalo E; Laboratorio de Biología Periodontal, Facultad de Odontología, Universidad Nacional Autónoma de México, Mexico City, Mexico.
Jazyk: angličtina
Zdroj: Journal of peptide science : an official publication of the European Peptide Society [J Pept Sci] 2023 Oct; Vol. 29 (10), pp. e3494. Date of Electronic Publication: 2023 Apr 29.
DOI: 10.1002/psc.3494
Abstrakt: We report the characterization of the three-dimensional structure of the CEMP1-p1 peptide [MGTSSTDSQQAQHRRCSTSN: corresponding to residues 1-20 of the N-terminus of cementum protein 1 (CEMP1)]. This peptide imitates the capacity of CEMP1 to stimulate hydroxyapatite (HA) crystal nucleation and growth, and promotes the differentiation of periodontal ligament cells into a cementoblastic phenotype. Additionally, in experimental models of critical-sized calvarial defects in Wistar rats, CEMP1-p1 has shown osteogenic properties that enhanced the physiological deposition and maturation of newly formed bone. In this work, studies of CEMP1-p1 by circular dichroism (CD) and nuclear magnetic resonance (NMR) were performed in trifluoroethanol D2 (TFED2) and aqueous solution to determine the 3D structure of the peptide. Using the 3D model, experimental data from HA crystals formation and calcium fluorescence emission, we explain the biological mechanisms involved in CEMP1-p1 activity to promote calcium recruitment and its affinity to HA crystals. This information is valuable because it proposes, for the first time, a plausible molecular mechanism during the mineralization process, from a specific cementum protein-derived peptide.
(© 2023 The Authors. Journal of Peptide Science published by European Peptide Society and John Wiley & Sons Ltd.)
Databáze: MEDLINE
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