Evolutionary Screening of Collagen-like Peptides That Nucleate Hydroxyapatite CrystalsOrthopedics and Physical Rehabilitation Publications and Presentations
UMMS AffiliationDepartment of Orthopedics and Physical Rehabilitation; Department of Cell Biology
Medical Subject HeadingsBiocompatible Materials; Bone Substitutes; Osteogenesis; Tissue Scaffolds; Hydroxyapatites
AbstractThe biogenesis of inorganic/organic composite materials such as bone typically involves the process of templated mineralization. Biomimetic synthesis of bone-like materials therefore requires the development of organic scaffolds that mediate mineralization of hydroxyapatite (HAP), the major inorganic component of bone. Using phage display, we identified a 12-residue peptide that bound to single-crystal HAP and templated the nucleation and growth of crystalline HAP mineral in a sequence- and composition-dependent manner. The sequence responsible for the mineralizing activity resembled the tripeptide repeat (Gly-Pro-Hyp) of type I collagen, a major component of bone extracellular matrix. Using a panel of synthetic peptides, we defined the structural features required for mineralizing activity. The results support a model for the cooperative noncovalent interaction of the peptide with HAP and suggest that native collagen may have a mineral-templating function in vivo. We expect this short HAP-binding peptide to be useful in the synthesis of three-dimensional bone-like materials.
Rights and PermissionsCitation: Langmuir. 2011 Jun 21;27(12):7620-8. Epub 2011 Feb 3. Link to article on publisher's site
Related ResourcesLink to Article in PubMed
Citation InformationWoo-Jae Chung, Ki-Young Kwon, Jie Song and Seung-Wuk Lee. "Evolutionary Screening of Collagen-like Peptides That Nucleate Hydroxyapatite Crystals" Vol. 27 Iss. 12 (2011) ISSN: 0743-7463 (Linking)
Available at: http://works.bepress.com/jie_song/20/