Abstract
The third-stage larvae (L3) of the filarid parasite Brugia pahangi were surveyed for protease activity beginning with release from the mosquito vector through molting to the fourth-stage larvae (L4). A metalloaminopeptidase with a substrate preference for phenylalanine was released during the molting process. A screen of aminopeptidase inhibitors identified H-boroPhenylalanine-(pinacol) as highly effective, with a Ki of 1.3 x 10(-11) M. This peptidase inhibitor also arrested molting of L3 larvae in vitro at a concentration of 100 microM.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Aminopeptidases / antagonists & inhibitors
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Aminopeptidases / isolation & purification
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Aminopeptidases / metabolism*
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Animals
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Boron Compounds / pharmacology
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Brugia pahangi / enzymology*
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Brugia pahangi / growth & development
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Glycopeptides / pharmacology
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Hydrogen-Ion Concentration
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Larva / enzymology
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Molecular Sequence Data
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Molecular Weight
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Oligopeptides / pharmacology
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Phenylalanine / metabolism
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Substrate Specificity
Substances
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Boron Compounds
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Glycopeptides
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H-borophenylalanyl-(pinacol)
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Oligopeptides
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Phenylalanine
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Aminopeptidases
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phosphoramidon