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Antithrombin-binding oligosaccharides: structural diversities in a unique function?

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Abstract

Heparin-antithrombin interaction is one of the most documented examples of heparin/protein complexes. The specific heparin sequence responsible for the binding corresponds to a pentasaccharide sequence with an internal 3-O-sulfated glucosamine residue. Moreover, the position of the pentasaccharide along the chain as well as the structure of the neighbor units affects the affinity to antithrombin. The development of separation and purification techniques, in conjunction with physico-chemical approaches (mostly NMR), allowed to characterize several structural variants of antithrombin-binding oligosaccharides, both in the free state and in complex with antithrombin. The article provides an overview of the studies that lead to the elucidation of the mechanism of interaction as well as acquiring new knowledge in heparin biosynthesis.

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Acknowledgments

We thank Drs. Benito Casu and Giuseppe Cassinelli for their critical reading of the manuscript and helpful comments.

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Authors and Affiliations

  1. Istituto di Ricerche Chimiche e Biochimiche “G. Ronzoni”, via G. Colombo 81, 20133, Milan, Italy

    Marco Guerrini & Giangiacomo Torri

  2. Sanofi, 13 Quai Jules Guesde, 94403, Vitry sur Seine, France

    Pierre A. J. Mourier & Christian Viskov

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  1. Marco Guerrini
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  2. Pierre A. J. Mourier
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  3. Giangiacomo Torri
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  4. Christian Viskov
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Correspondence to Marco Guerrini.

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Guerrini, M., Mourier, P.A.J., Torri, G. et al. Antithrombin-binding oligosaccharides: structural diversities in a unique function?. Glycoconj J 31, 409–416 (2014). https://doi.org/10.1007/s10719-014-9543-9

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