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.
Wood, Bayden R.
中科院分区:
生物学3区
文献类型:
--
作者:
Egan, Timothy J.;Chen, Jeff Y-J.;Wood, Bayden R.

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包括疟原虫在内的几种吸血生物通过将宿主血红蛋白释放的血红素转化为不溶性结晶铁原卟啉IX二聚体(称为疟原虫色素)来解毒。迄今为止,虽然脂质或蛋白质被认为可以催化其形成,但疟原虫色素的形成机制仍不清楚。我们已经发现,β-血红素(合成的疟原虫色素)迅速形成的生理现实条件下,辛醇/水,戊醇/水和脂质/水界面附近。分子动力学模拟表明,在没有水的竞争氢键的情况下,疟原虫色素二聚体的前体自发形成,表明这种物质可能在体内脂质/水界面附近自组装。(c)2006年欧洲生物化学学会联合会。Elsevier B. V.出版,保留所有权利。
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.