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Identification of potential targets for an anticoagulant pectin.

Identifieur interne : 000168 ( Main/Exploration ); précédent : 000167; suivant : 000169

Identification of potential targets for an anticoagulant pectin.

Auteurs : Aline Guimarães Santana [Brésil] ; Ana Helena Pereira Gracher [Brésil] ; André Luis Rüdiger [Brésil] ; Nilson Ivo Tonin Zanchin [Brésil] ; Paulo Costa Carvalho [Brésil] ; Thales Ricardo Cipriani [Brésil] ; Tatiana De Arruda Campos Brasil De Souza [Brésil]

Source :

Journal of proteomics [ 1876-7737 ] ; 2016.

RBID : pubmed:27318178

Abstract

Heparin is a sulfated polysaccharide of animal origin showing excellent anticoagulant properties. Although it strongly inhibits the coagulation cascade, its interaction with multiple sites results in several side effects. An ideal alternative compound should not only possess anticoagulant and antithrombotic activities, but also provide specific binding to components of the coagulation cascade to decrease side effects and facilitate the control of pharmacologic actions in patient's body. In this work, we performed a scan of potential targets for chemically sulfated pectin from Citrus sinensis (SCP) that shows an efficient anticoagulant activity by combining proteomics and molecular docking techniques. Defining the interaction partners of SCP is fundamental to evaluate if its pharmacological side effects can be as harmful as those from heparin. SCP interacts directly with heparin cofactor II, probably favoring its interaction with thrombin. SCP interaction with antithrombin depends likely on its association with thrombin or factor Xa. In addition to the interaction with factors related to homeostasis, SCP may also act on the renin-angiotensin and on the complement systems.

DOI: 10.1016/j.jprot.2016.06.013
PubMed: 27318178

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en">Heparin is a sulfated polysaccharide of animal origin showing excellent anticoagulant properties. Although it strongly inhibits the coagulation cascade, its interaction with multiple sites results in several side effects. An ideal alternative compound should not only possess anticoagulant and antithrombotic activities, but also provide specific binding to components of the coagulation cascade to decrease side effects and facilitate the control of pharmacologic actions in patient's body. In this work, we performed a scan of potential targets for chemically sulfated pectin from Citrus sinensis (SCP) that shows an efficient anticoagulant activity by combining proteomics and molecular docking techniques. Defining the interaction partners of SCP is fundamental to evaluate if its pharmacological side effects can be as harmful as those from heparin. SCP interacts directly with heparin cofactor II, probably favoring its interaction with thrombin. SCP interaction with antithrombin depends likely on its association with thrombin or factor Xa. In addition to the interaction with factors related to homeostasis, SCP may also act on the renin-angiotensin and on the complement systems.</div>
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Identification of potential targets for an anticoagulant pectin.

Identification of potential targets for an anticoagulant pectin.

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