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The critical role of membranes in haemozin crystal assembly and the mode of action of antimalarial drugs

Reference	BBS/B/05508
Principal Investigator / Supervisor	Dr Patrick Bray
Co-Investigators / Co-Supervisors	Dr Richard Bonar-Law, Prof. Paul ONeill, Professor Stephen Ward
Institution	University of Liverpool
Department	Liverpool School of Tropical Medicine
Funding type	Research
Value (£)	299,489
Status	Completed
Type	Research Grant
Start date	01/03/2004
End date	28/02/2007
Duration	36 months

Abstract

Degradation of haemoglobin by malaria parasites releases ferriprotoporphyrin IX (FP) which is detoxified by crystallisation into haemozoin (HZ). Antimalarial drugs bind to FP and corrupt this process. The basic cell biology and chemistry of these linked events, which occur at the membrane / water interface, are poorly characterised. Consequently HZ formation cannot be adequately explained within the timeframe of parasite development. Neither can drug activity be adequately predicted from current binding data. We propose first investigation of crystal biogenesis in membranes using synthetic FP dimers, in vitro crystallisation assays, and axenic cultures. FP-drug interactions in membranes and vesicles will be measured spectroscopically.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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