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

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.

Duke Scholars

Author Matthew L Becker Chemistry