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A group of inactivators of cysteinyl proteinases which function by covalent bond formation have been examined for their ability to inhibit the development of Plasmodium falciparum within red blood cells. The most effective of these caused inactivation of the parasite near 10(-8) M concentration. The range of inhibitory action varied with peptide structure in a manner characteristic of affinity labels for proteinases suggesting that the target of inhibition was an unidentified proteinase, probably of the cysteinyl type, but different from cathepsins B and L.

Original publication

DOI

10.1016/0014-5793(90)80022-b

Type

Journal article

Journal

FEBS letters

Publication Date

01/1990

Volume

259

Pages

257 - 259

Addresses

Dept. of Immunology, University College and Middlesex Hospital Medical School, London, England.

Keywords

Erythrocytes, Animals, Humans, Plasmodium falciparum, Dipeptides, Protease Inhibitors, Structure-Activity Relationship