title: Evolutionary screening of collagen-like peptides that nucleate hydroxyapatite crystals.
abstract: The 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.
authors.affiliation: Department of Bioengineering, University of California, Berkeley, Berkeley, California 94720, USA.
authors.forename: Woo-Jae
authors.initials: WJ
authors.lastname: Chung
authors.forename: Ki-Young
authors.initials: KY
authors.lastname: Kwon
authors.forename: Jie
authors.initials: J
authors.lastname: Song
authors.forename: Seung-Wuk
authors.initials: SW
authors.lastname: Lee
mesh_terms: D003094:Collagen / Q000737:chemistry*; D003460:Crystallization; D017886:Durapatite / Q000737:chemistry*; D019418:Evolution, Chemical; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*
chemical_list: D010455:Peptides; D003094:Collagen; D017886:Durapatite