4.5 Review

Re-visiting the structure of heparin

Journal

CARBOHYDRATE RESEARCH
Volume 403, Issue -, Pages 60-68

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.carres.2014.06.023

Keywords

Heparin structure; Active site for antithrombin; Low-molecular-weight heparins; Heparin oligosaccharides; Protein binding; Conformations

Funding

  1. National Institutes of Health, United States [R01-CA138535]
  2. Finlombardia SpA, Italy (Fondo promozione accordi istituzionali)

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The sulfated polysaccharide heparin has been used as a life-saving anticoagulant in clinics well before its detailed structure was known. This mini-review is a survey of the evolution in the discovery of the primary and secondary structure of heparin. Highlights in this history include elucidation and synthesis of the specific sequence that binds to antithrombin, the development of low-molecular-weight heparins currently used as antithrombotic drugs, and the most promising start of chemo-enzymatic synthesis. Special emphasis is given to peculiar conformational properties contributing to interaction with proteins that modulate different biological properties. (C) 2014 Elsevier Ltd. All rights reserved.

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