Haemozoin (beta-haematin) biomineralization occurs by self-assembly near the lipid/water interface.
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.
Egan
Timothy J
TJ
Department of Chemistry, University of Cape Town, Private Bag, Rondebosch 7701, South Africa. tegan@science.uct.ac.za
Chen
Jeff Y-J
JY
de Villiers
Katherine A
KA
Mabotha
Tebogo E
TE
Naidoo
Kevin J
KJ
Ncokazi
Kanyile K
KK
Langford
Steven J
SJ
McNaughton
Don
D
Pandiancherri
Shveta
S
Wood
Bayden R
BR
D000818:Animals; D006420:Hemeproteins / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D007700:Kinetics; D008055:Lipids / Q000737:chemistry*; D008958:Models, Molecular; D010963:Plasmodium falciparum / Q000737:chemistry; D013055:Spectrophotometry, Infrared; D013059:Spectrum Analysis, Raman; D014867:Water / Q000737:chemistry*; D014961:X-Ray Diffraction
D006420:Hemeproteins; D008055:Lipids; D014867:Water; C020753:hemozoin