Heparin is comprised of long, unbranched, anionic polysaccharide chains.  Although its basic structure consists of a repeating disaccharide unit of uronic acid and glucosamine, heparin is microhetergeneous due to various patterns of sulfonation and epimerization.  Heparin is a widely used anticoagulant, acting through the binding of a specific pentasaccharide sequence to the protease inhibitor antithrombin III.  It has also been shown to interact with various other proteins.  To study its structure and interactions with these proteins, it must first be depolymerized, which produces oligosaccharides of various chain lengths.  Recent studies have suggested the hydroxy and sulfamate protons can provide new information regarding the heparin structure and of the nature of their protein interactions.  By measuring and comparing their temperature coefficients and exchange activation energies by 1H NMR, we can determine which of these protons participate in hydrogen bonding.  Oligosaccharides studied include Arixtra and enzymatically digested heparin tetrasaccharides.

NMR analysis of heparin hydroxy and sulfamate protons

243rd National Meeting (2012)

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