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Quantification of the binding affinity of a specific hydroxyapatite binding peptide.

Publication ,  Journal Article
Weiger, MC; Park, JJ; Roy, MD; Stafford, CM; Karim, A; Becker, ML
Published in: Biomaterials
April 2010

The genesis of bone and teeth involves highly coordinated processes, which involve multiple cell types and proteins that direct the nucleation and crystallization of inorganic hydroxyapatite (HA). Recent studies have shown that peptides mediate the nucleation process, control HA microstructure or even inhibit HA mineralization. Using phage display technology, a short peptide was identified that binds to crystalline HA and to HA-containing domains of human teeth with chemical and morphological specificity. However, the binding affinity and specific amino acids that significantly contribute to this interaction require further investigation. In this study, we employ a microfluidic chip based surface plasmon resonance imaging (SPRi) technique to quantitatively measure peptide affinity by fabricating a novel 4 layer HA SPR sensor. We find the peptide (SVSVGMKPSPRPGGGK) binds with relatively high affinity (K(D) = 14.1 microM +/- 3.8 microM) to HA. The independently measured amino acid fragment SVSV seems to impart a significant contribution to this interaction while the MKPSP fragment may provide a conformational dependent component that enhances the peptides affinity but by itself shows little specificity in the current context. These data show that together, the two moieties promote a stronger synergistic binding interaction to HA than the simple combination of the individual components.

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Published In

Biomaterials

DOI

EISSN

1878-5905

ISSN

0142-9612

Publication Date

April 2010

Volume

31

Issue

11

Start / End Page

2955 / 2963

Related Subject Headings

  • Tooth
  • Surface Plasmon Resonance
  • Protein Binding
  • Peptides
  • Peptide Library
  • Peptide Fragments
  • Molecular Sequence Data
  • Microfluidic Analytical Techniques
  • Humans
  • Durapatite
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Weiger, M. C., Park, J. J., Roy, M. D., Stafford, C. M., Karim, A., & Becker, M. L. (2010). Quantification of the binding affinity of a specific hydroxyapatite binding peptide. Biomaterials, 31(11), 2955–2963. https://doi.org/10.1016/j.biomaterials.2010.01.012
Weiger, Michael C., Jung Jin Park, Marc D. Roy, Christopher M. Stafford, Alamgir Karim, and Matthew L. Becker. “Quantification of the binding affinity of a specific hydroxyapatite binding peptide.Biomaterials 31, no. 11 (April 2010): 2955–63. https://doi.org/10.1016/j.biomaterials.2010.01.012.
Weiger MC, Park JJ, Roy MD, Stafford CM, Karim A, Becker ML. Quantification of the binding affinity of a specific hydroxyapatite binding peptide. Biomaterials. 2010 Apr;31(11):2955–63.
Weiger, Michael C., et al. “Quantification of the binding affinity of a specific hydroxyapatite binding peptide.Biomaterials, vol. 31, no. 11, Apr. 2010, pp. 2955–63. Epmc, doi:10.1016/j.biomaterials.2010.01.012.
Weiger MC, Park JJ, Roy MD, Stafford CM, Karim A, Becker ML. Quantification of the binding affinity of a specific hydroxyapatite binding peptide. Biomaterials. 2010 Apr;31(11):2955–2963.
Journal cover image

Published In

Biomaterials

DOI

EISSN

1878-5905

ISSN

0142-9612

Publication Date

April 2010

Volume

31

Issue

11

Start / End Page

2955 / 2963

Related Subject Headings

  • Tooth
  • Surface Plasmon Resonance
  • Protein Binding
  • Peptides
  • Peptide Library
  • Peptide Fragments
  • Molecular Sequence Data
  • Microfluidic Analytical Techniques
  • Humans
  • Durapatite