Plasmodium chabaudi chabaudi and P. falciparum: inhibition of aminopeptidase and parasite growth by bestatin and nitrobestatin.
Parasitol Res
; 84(7): 552-8, 1998 Jul.
Article
em En
| MEDLINE
| ID: mdl-9694371
ABSTRACT
The major leucine aminopeptidase of the rodent malarial parasite Plasmodium chabaudi chabaudi was partially purified using a combination of high-pressure liquid chromatography on a size-exclusion column and affinity chromatography using the aminopeptidase-specific inhibitor bestatin as the ligand. The purified enzyme showed simple Michaelis-Menten kinetics when the fluorogenic peptide analogue leucyl-7-amino-4-methyl-courmarin served as the substrate, and it was strongly inhibited by both bestatin (Ki = 50.7 +/- 21.0 nM) and nitrobestatin (Ki = 2.51 +/- 0.2 nM) in a competitive manner. These inhibitors were also potent blockers of the growth of P. c. chabaudi and the human parasite P. falciparum in culture, and nitrobestatin was again the more potent. Therefore, the leucine aminopeptidase represents an important target to which novel anti-malarial agents could be directed.
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Base de dados:
MEDLINE
Assunto principal:
Plasmodium falciparum
/
Plasmodium chabaudi
/
Leucina
/
Leucil Aminopeptidase
/
Antimaláricos
Idioma:
En
Ano de publicação:
1998
Tipo de documento:
Article