Haemozoin (β-haematin) biomineralization occurs by self-assembly near the lipid/water interface
Haemozoin (β-haematin) biomineralization occurs by self-assembly near the lipid/water interface
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DOI:
10.1016/j.febslet.2006.08.043
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发表时间:
2006-09-18
期刊:
影响因子:
3.5
通讯作者:
Wood, Bayden R.
中科院分区:
文献类型:
--
作者:
Egan, Timothy J.;Chen, Jeff Y-J.;Wood, Bayden R.
Several blood-feeding organisms, including the malaria parasite detoxify haem released from host haemoglobin by conversion to the insoluble crystalline ferriprotoporphyrin IX dimer known as haemozoin. To date the mechanism of haemozoin formation has remained unknown, although lipids or proteins have been suggested to catalyse its formation. We have found that beta-haematin (synthetic haemozoin) forms rapidly under physiologically realistic conditions near octanol/water, pentanol/ water and lipid/water interfaces. Molecular dynamics simulations show that a precursor of the haemozoin dimer forms spontaneously in the absence of the competing hydrogen bonds of water, demonstrating that this substance probably self-assembles near a lipid/water interface in vivo. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.