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Analytical and Bioanalytical Chemistry

, Volume 406, Issue 13, pp 3079–3089 | Cite as

Characterization of heparin–protein interaction by saturation transfer difference (STD) NMR

  • Fei Yu
  • Sucharita Roy
  • Enrique Arevalo
  • John Schaeck
  • Jason Wang
  • Kimberly Holte
  • Jay Duffner
  • Nur Sibel Gunay
  • Ishan Capila
  • Ganesh V. Kaundinya
Research Paper

Abstract

The binding affinity and specificity of heparin to proteins is widely recognized to be sulfation-pattern dependent. However, for the majority of heparin-binding proteins (HBPs), it still remains unclear what moieties are involved in the specific binding interaction. Here, we report our study using saturation transfer difference (STD) nuclear magnetic resonance (NMR) to map out the interactions of synthetic heparin oligosaccharides with HBPs, such as basic fibroblast growth factor (FGF2) and fibroblast growth factor 10 (FGF10), to provide insight into the critical epitopes of heparin ligands involved. The irradiation frequency of STD NMR was carefully chosen to excite the methylene protons so that enhanced sensitivity was obtained for the heparin–protein complex. We believe this approach opens up additional application avenues to further investigate heparin–protein interactions.

Keywords

Heparin Saturation transfer difference NMR Binding epitope FGF2 FGF10 Surface plasmon resonance 

Notes

Acknowledgment

The authors would like to thank Dr. Desiree Tsao for sharing her expertise in STD NMR.

Supplementary material

216_2014_7729_MOESM1_ESM.pdf (3.4 mb)
ESM 1 (PDF 3519 kb)

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Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  • Fei Yu
    • 1
  • Sucharita Roy
    • 1
  • Enrique Arevalo
    • 1
  • John Schaeck
    • 1
  • Jason Wang
    • 1
  • Kimberly Holte
    • 1
  • Jay Duffner
    • 1
  • Nur Sibel Gunay
    • 1
  • Ishan Capila
    • 1
  • Ganesh V. Kaundinya
    • 1
  1. 1.Momenta PharmaceuticalsCambridgeUSA

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