Study on Interactions of Oligo(tyrosine sulfate)s with Synthetic Heparin-binding Peptides by Affinity Chromatography and MALDI-TOF-MS
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...
KeywordsBinding Affinity Residue Number Relative Binding Affinity Surface Plasmon Resonance Spectroscopy Tyrosine Sulfate
One of us (MY) is indebted to support from the Hayashi Memorial Foundation for Female Natural Scientists.