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Cementomimetics——constructing a cementum-like biomineralized microlayer via amelogenin-derived peptides

International Journal of Oral Science 2012年第2期4卷 69-77页

作者： Mustafa Gungormus Ersin E Oren Jeremy A Horst Hanson Fong Marketa Hnilova Martha J Somerman Malcolm L Snead Ram Samudrala Candan Tamerler Mehmet Sarikaya Genetically Engineered Materials Science and Engineering Center and Department of Materials Science and EngineeringUniversity of WashingtonSeattleUSA Departmentof Orofacial Sciences University of California at San FranciscoSan FranciscoUSA Laboratory of Oral Connective Tissue Biology National Institute of Arthritis and Musculoskeletal and Skin DiseasesNational Institutes of HealthBethesdaUSA Center for Craniofacial Molecular Biology Ostrow School of Dentistry of the University of Southern CaliforniaLos AngelesUSA Department of Microbiology University of WashingtonSeattleUSA

Cementum is the outer-, mineralized-tissue covering the tooth root and an essential part of the system of periodontal tissue that anchors the tooth to the bone. Periodontal disease results from the destructive behavior of the host elicited by an infectious biofilm adhering to the tooth root and left untreated, may lead to tooth loss. We describe a novel protocol for identifying peptide sequences from native proteins with the potential to repair damaged dental tissues by controlling hydroxyapatite biomineralization. Using amelogenin as a case study and a bioinformatics scoring matrix, we identified regions within amelogenin that are shared with a set of hydroxyapatite-binding peptides （HABPs） previously selected by phage display. One 22-amino acid long peptide regions referred to as amelogenin-derived peptide 5 （ADP5） was shown to facilitate cell-free formation of a cementum-like hydroxyapatite mineral layer on demineralized human root dentin that, in turn, supported attachment of periodontal ligament cells in vitro. Our findings have several implications in peptide-assisted mineral formation that mimic biomineralization. By further elaborating the mechanism for protein control over the biomineral formed, we afford new insights into the evolution of protein-mineral interactions. By exploiting small peptide domains of native proteins, our understanding of structure-function relationships of biomineralizing proteins can be extended and these peptides can be utilized to engineer mineral formation. Finally, the cementomimetic layer formed by ADP5 has the potential clinical application to repair diseased root surfaces so as to promote the regeneration of periodontal tissues and thereby reduce the morbiditv associated with tooth loss.

关键词： amelogenin amelogenin-derived peptides bioinformatics biomineralization cementomimetics cementum demineral-ization remineralization

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