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Study on Interactions of Oligo(tyrosine sulfate)s with Synthetic Heparin-binding Peptides by Affinity Chromatography and MALDI-TOF-MS

  • Miyuki Yamaguchi
  • Masaaki Ueki
Conference paper
Part of the Advances in Experimental Medicine and Biology book series (volume 611)

Introduction

The heparin/heparan sulfate-like glycosaminoglycans (HLGAGs) play important roles in the regulation of many biological processes. However, a controlled application has been limited because of their heterogeneity and difficulty in synthesis. To solve the problems, many synthetic mimics including sulfated peptides have been prepared. Since the discovery of anti-HIV activity in oligo(tyrosine sulfate)s in our laboratory [1, 2], we have been interested in their potential as HLGAG mimics. In this study, we investigated their interactions with synthetic heparin-binding peptides using affinity chromatography and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS).

Results and Discussion

Binding affinities of the heparin-binding peptides were preliminarily compared by retention on a NaO3S-[Tyr(SO3Na)]9-immobilized affinity column and a H-[Tyr(SO3Na)]9-immobilized affinity column in the presence of increasing NaCl concentrations. Four...

Keywords

Binding Affinity Residue Number Relative Binding Affinity Surface Plasmon Resonance Spectroscopy Tyrosine Sulfate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Notes

Acknowledgments

One of us (MY) is indebted to support from the Hayashi Memorial Foundation for Female Natural Scientists.

References

  1. 1.
    Ueki, M., et al. Bioorg. Med. Chem., 9, 477–486 (2001).CrossRefGoogle Scholar
  2. 2.
    Ueki, M., et al. Bioorg. Med. Chem., 9, 487–492 (2001).CrossRefGoogle Scholar
  3. 3.
    Onoue, S., et al. Peptides, 24, 821–826 (2003).CrossRefGoogle Scholar
  4. 4.
    Liu, S., et al. Proc. Natl. Acad. Sci. USA, 94, 1739–1744 (1997).CrossRefGoogle Scholar
  5. 5.
    Kaiser, N., et al. Nature Med., 7, 123–128 (2001).CrossRefGoogle Scholar
  6. 6.
    Ueki, M. and Yamaguchi, M. Rapid Commun. Mass Spectrom., 20, 1615–1620 (2006).CrossRefGoogle Scholar
  7. 7.
    Maynard, H. D. and Hubbell, J. A. Acta Biomaterialia, 1, 451–459 (2005).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  • Miyuki Yamaguchi
    • 1
  • Masaaki Ueki
    • 1
  1. 1.Department of Applied ChemistryTokyo University of ScienceTokyoJapan

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