Evolutionary Screening of Collagen-like Peptides That Nucleate Hydroxyapatite Crystals

Citations

WEB OF SCIENCE

68
Citations

SCOPUS

80

초록

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.

키워드

AMPHIPHILE NANOFIBERS; BINDING PEPTIDES; PHAGE DISPLAY; IN-VITRO; MINERALIZATION; RESOLUTION; SELECTION; AFFINITY; APATITE; NANOPARTICLES
제목
Evolutionary Screening of Collagen-like Peptides That Nucleate Hydroxyapatite Crystals
저자
Chung, Woo-Jae; Kwon, Ki-Young; Song, Jie; Lee, Seung-Wuk
DOI
10.1021/la104757g
발행일
2011-06-21
유형
Article
저널명
Langmuir
권
27
호
12
페이지
7620 ~ 7628