Identification of a highly specific hydroxyapatite-binding peptide using phage display

Published

Journal Article

A study was conducted to identify a peptide sequence that show high-specific binding to crystalline hydroxyaptite. Hydroxyapatite is used to provide stationary phase in the chromatographic purification of amplified phage. The study used x-ray diffraction (XRD) analysis to determine the crystallinity. The hydroxyapatite materials was blocked during the study from phage adhesion by pre-incubating with bovine serum albumin (BSA). The study also used a quartz crystal microbalance measurement with dissipation (QCM-D) to determine the binding of phage displaying peptide. A C-terminal biotinylated HA 6-1 peptide and SVSVGMKPSPRP-biotin was incubated during the study with BSA-blocked substrates. The study concluded that this peptide can be used for various biological applications including biomineralization of HA.

Full Text

Duke Authors

Cited Authors

  • Roy, MD; Stanley, SK; Amis, EJ; Becker, ML

Published Date

  • May 19, 2008

Published In

Volume / Issue

  • 20 / 10

Start / End Page

  • 1830 - 1836

International Standard Serial Number (ISSN)

  • 0935-9648

Digital Object Identifier (DOI)

  • 10.1002/adma.200702322

Citation Source

  • Scopus