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Inhibition of intraerythrocytic development of Plasmodium falciparum by proteinase inhibitors
Author(s) -
Rockett K.A.,
Playfair J.H.L.,
Ashall F.,
Target G.A.T.,
Angliker H.,
Shaw E.
Publication year - 1990
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 - 10.1016/0014-5793(90)80022-b
Subject(s) - plasmodium falciparum , peptide , biochemistry , cysteine proteinase inhibitors , parasite hosting , cathepsin , cysteine , enzyme , chemistry , covalent bond , biology , malaria , immunology , apoptosis , organic chemistry , programmed cell death , world wide web , computer science , caspase
A group of inactivators of cysteinyl proteinases which function by covalent bond formation have been examined for their ability to inhibit thedevelopment 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.