Heparin dodecasaccharide containing two antithrombin-binding pentasaccharides: structural features and biological properties

J Biol Chem. 2013 Sep 6;288(36):25895-25907. doi: 10.1074/jbc.M113.485268. Epub 2013 Jul 10.

Abstract

The antithrombin (AT) binding properties of heparin and low molecular weight heparins are strongly associated to the presence of the pentasaccharide sequence AGA*IA (A(NAc,6S)-GlcUA-A(NS,3,6S)-I(2S)-A(NS,6S)). By using the highly chemoselective depolymerization to prepare new ultra low molecular weight heparin and coupling it with the original separation techniques, it was possible to isolate a polysaccharide with a biosynthetically unexpected structure and excellent antithrombotic properties. It consisted of a dodecasaccharide containing an unsaturated uronate unit at the nonreducing end and two contiguous AT-binding sequences separated by a nonsulfated iduronate residue. This novel oligosaccharide was characterized by NMR spectroscopy, and its binding with AT was determined by fluorescence titration, NMR, and LC-MS. The dodecasaccharide displayed a significantly increased anti-FXa activity compared with those of the pentasaccharide, fondaparinux, and low molecular weight heparin enoxaparin.

Keywords: 3-O-Sulfation; Antithrombin; Glycosaminoglycan; Heparin; Mass Spectrometry (MS); NMR.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbohydrate Sequence
  • Factor Xa / chemistry*
  • Fibrinolytic Agents* / chemical synthesis
  • Fibrinolytic Agents* / chemistry
  • Heparin
  • Humans
  • Magnetic Resonance Spectroscopy
  • Oligosaccharides* / chemical synthesis
  • Oligosaccharides* / chemistry

Substances

  • Fibrinolytic Agents
  • Oligosaccharides
  • Heparin
  • Factor Xa