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Polyelectrolyte Complex for Heparin Binding Domain Osteogenic Growth Factor Delivery
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Interactions between nattokinase and heparin/GAGs.

Fuming Zhang1, Jianhua Zhang2,3, Robert J Linhardt4,5,6,7

  • 1Department of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA.

Glycoconjugate Journal
|September 29, 2015
PubMed
Summary
This summary is machine-generated.

Nattokinase (NK), a fibrinolytic enzyme, binds to heparin and other glycosaminoglycans. This interaction is chain-length dependent and crucial for NK

Keywords:
BindingHeparinNattokinaseSurface plasmon resonance

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Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Nattokinase (NK) is a serine protease from natto with fibrinolytic and thrombolytic properties.
  • NK is explored as a nutraceutical for oral thrombolytic therapy and other conditions like hypertension and Alzheimer's disease.
  • Heparin and its derivatives are key anticoagulants, modulating protein interactions and enzyme activities.

Purpose of the Study:

  • To investigate the interaction between Nattokinase (NK) and heparin using surface plasmon resonance spectroscopy.
  • To determine the binding affinity, chain-length dependency, and essential structural features of heparin for NK interaction.
  • To assess NK's interaction with other glycosaminoglycans (GAGs) and its effect on other heparin-protein interactions.

Main Methods:

  • Surface Plasmon Resonance (SPR) spectroscopy was employed to study NK-heparin interactions.
  • Varying sizes of heparin oligosaccharides and chemically modified heparins were used to analyze binding characteristics.
  • Binding affinities to other GAGs (HS, DS, CSE) and interference with heparin-protein interactions were evaluated.

Main Results:

  • Nattokinase (NK) exhibits heparin-binding protein characteristics with an affinity of approximately 250 nM.
  • The interaction is dependent on heparin chain length, with a minimum binding size of a hexasaccharide.
  • Heparin's 6-O-sulfo and N-sulfo groups are essential for binding, while 2-O-sulfo groups are not.
  • NK showed modest binding to other GAGs and interfered with heparin's interactions with antithrombin and fibroblast growth factors.

Conclusions:

  • Nattokinase (NK) binds to heparin in a chain-length-dependent manner, requiring specific sulfation patterns.
  • These findings provide insights into NK's mechanism of action and potential therapeutic applications involving heparin.
  • NK's ability to modulate other heparin-protein interactions suggests broader physiological relevance.