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Glycosaminoglycan-directed cobalt complexes.

Jessica M Christian1, Mary Zoepfl1, Wyatt E Johnson2

  • 1Department of Chemistry, Virginia Commonwealth University, 1001 W Main St, Richmond, VA 23284, United States of America.

Journal of Inorganic Biochemistry
|May 14, 2023
PubMed
Summary
This summary is machine-generated.

Simple cobalt (Co) compounds interact with glycosaminoglycans (GAGs), like heparan sulfate (HS). One Co complex, [CoCl(NH3)5]2+, inhibits bacterial heparinase and cell invasion, revealing novel biological activity.

Keywords:
Cellular invasionCobaltFondaparinuxGlycosaminoglycansHeparinase inhibitionMetalloglycomics

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Area of Science:

  • Bioinorganic Chemistry
  • Glycosaminoglycan Interactions
  • Metalloglycomics

Background:

  • Werner's Complex, containing cobalt (Co), exhibits biological activity linked to glycosaminoglycans (GAGs) such as heparan sulfate (HS).
  • Understanding the molecular basis of these interactions is crucial for exploring novel therapeutic applications.

Purpose of the Study:

  • To investigate the interactions between simple mononuclear Co(III) compounds and HS, using Fondaparinux (FPX) as a model.
  • To explore the potential for substitution-inert and covalently binding Co complexes in biological systems.

Main Methods:

  • Indirect competitive inhibition assays and direct mass spectrometry were employed to study Co complex-FPX interactions.
  • Mass spectrometry confirmed covalent binding of specific Co-Cl complexes.

Main Results:

  • Formally substitution-inert Co complexes demonstrated binding to FPX, with metalloshielding protecting against sulfate loss.
  • Covalent binding of [CoCl(NH3)5]2+ and cis-[CoCl2(en)2]+ was confirmed.
  • [CoCl(NH3)5]2+ effectively inhibited bacterial heparinase and heparanase-dependent cellular invasion.

Conclusions:

  • Simple mononuclear cobalt complexes can interact with and bind to glycosaminoglycans.
  • The compound [CoCl(NH3)5]2+ exhibits significant, previously unrecognized biological activity as a heparinase inhibitor and in blocking cell invasion.