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

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

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...

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Bibliographic Details
Published in:Journal of peptide science Vol. 29; no. 10; p. e3494
Main Authors: Campos, Mikado Nidome, Giraldo, Estefanía López, Del Rio Portilla, Federico, Fernández-Velasco, Daniel Alejandro, Arzate, Higinio, Romo-Arévalo, Enrique
Format: Journal Article
Language:English
Published: England Wiley Subscription Services, Inc 01-10-2023
Subjects:
Animal models
Aqueous solutions
Calcium
Cell differentiation
Cementum
Circular dichroism
Crystal defects
Crystal growth
Crystals
Dichroism
Fluorescence
Hydroxyapatite
Mineralization
Molecular modelling
NMR
Nuclear magnetic resonance
Nucleation
Peptides
Periodontal ligament
Phenotypes
Protein structure
Proteins
Three dimensional models
Trifluoroethanol
NMR structure
CEMP1-p1
hydroxyapatite formation
biomineralization
cementum
cementum protein 1 synthetic peptide
periodontium
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Summary: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.
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ISSN:1075-2617
1099-1387
DOI:10.1002/psc.3494