Title

Evolutionary Screening of Collagen-like Peptides That Nucleate Hydroxyapatite Crystals

UMMS Affiliation

Department of Orthopedics and Physical Rehabilitation; Department of Cell Biology

Publication Date

2011-02-05

Document Type

Article

Subjects

Biocompatible Materials; Bone Substitutes; Osteogenesis; Tissue Scaffolds; Hydroxyapatites

Disciplines

Orthopedics | Rehabilitation and Therapy

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.

DOI of Published Version

10.1021/la104757g

Source

Langmuir. 2011 Jun 21;27(12):7620-8. Epub 2011 Feb 3. Link to article on publisher's site

Journal/Book/Conference Title

Langmuir : the ACS journal of surfaces and colloids

Related Resources

Link to Article in PubMed

PubMed ID

21291244

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