Researchers decipher mechanism by which anophelin binds to thrombin

Published on December 12, 2012 at 1:49 AM · No Comments

An international project lead by the Molecular and Cell Biology Institute of Porto University with the participation of researchers from IMIM (Hospital del Mar Medical Research Institute) has, for the first time ever, deciphered the mechanism by which a substance called anophelin binds to an enzyme (thrombin) involved in the process of blood coagulation. This discovery was published in the last issue of the PNAS journal and opens the door to, on the one hand, designing a new generation of anticoagulant drugs with a totally different functioning to current ones and, on the other hand, fighting against the spreading of malaria by designing inhibitors for this substance.

Anophelin is a substance playing a crucial role in the nutrition of a large number of parasites like malaria-carrying Anopheles mosquitoes or vampire bats. These animals need to feed on fresh blood and stop it from coagulating while they are eating. To make this possible, they use powerful inhibitors of the coagulation process mainly affecting thrombin. Researchers have discovered that "anophelin blocks thrombin in a new and different way than other substances: it's like a key fitting in a lock of a door, but in this case the key fits in the other side" explains Ricardo Guti-rrez Gallego, a member of the IMIM Bioanalysis research group.

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