Haemozoin (beta-haematin) biomineralization occurs by self-assembly near the lipid/water interface.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Egan TJ,Chen JY,de Villiers KA,Mabotha TE,Naidoo KJ,Ncokazi KK,Langford SJ,McNaughton D,Pandiancherri S,Wood BR

doi

10.1016/j.febslet.2006.08.043

subject

Has Abstract

pub_date

2006-09-18 00:00:00

pages

5105-10

issue

21

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)01019-2

journal_volume

580

pub_type

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