Valency-dependent affinity of bioactive hydroxyapatite-binding dendrons.

Published

Journal Article

Hydroxyapatite (HA)-coated surfaces are used widely as stationary phase for protein and enzyme purification, coatings for dental and orthopedic implants, and composite materials for tissue engineering substrates. More advanced applications are envisioned, but progress has been slowed by the limited ability to controllably functionalize the surface of HA with biomolecules in a translationally relevant manner. Herein we report the synthesis and characterization of a series of multivalent, HA-binding peptide bioconjugates with variable valency and tether length which afford the ability to precisely tune the desired binding behavior. The respective binding affinities of the multivalent constructs to HA surface were characterized by quartz crystal microbalance with dissipation monitoring (QCM-D) techniques, and the relationship between dendron structure and binding affinity was revealed. Tetravalent constructs of HA-binding peptides show a 100-fold enhancement in binding affinity compared to HA-binding peptide sequences reported previously. Both biotin and bone morphogenic protein-2 (BMP-2) derivative peptide were successfully linked to the focal point as initial demonstrations.

Full Text

Duke Authors

Cited Authors

  • Tang, W; Ma, Y; Xie, S; Guo, K; Katzenmeyer, B; Wesdemiotis, C; Becker, ML

Published Date

  • September 2013

Published In

Volume / Issue

  • 14 / 9

Start / End Page

  • 3304 - 3313

PubMed ID

  • 23931528

Pubmed Central ID

  • 23931528

Electronic International Standard Serial Number (EISSN)

  • 1526-4602

International Standard Serial Number (ISSN)

  • 1525-7797

Digital Object Identifier (DOI)

  • 10.1021/bm400908c

Language

  • eng