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Haemozoin (β‐haematin) biomineralization occurs by self‐assembly near the lipid/water interface
Author(s) -
Egan Timothy J.,
Chen Jeff Y-J.,
de Villiers Katherine A.,
Mabotha Tebogo E.,
Naidoo Kevin J.,
Ncokazi Kanyile K.,
Langford Steven J.,
McNaughton Don,
Pandiancherri Shveta,
Wood Bayden R.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.08.043
Subject(s) - dimer , chemistry , biophysics , hydrogen bond , biomineralization , biochemistry , molecule , biology , organic chemistry , paleontology
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 β‐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.