Bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases.

Authors :: Harbut, Michael B.
Velmourougane, Geetha
Dalal, Seema
Reiss, Gilana
Whisstock, James C.
Onder, Ozlem
Brisson, Dustin
McGowan, Sheena
Klemba, Michael
Greenbaum, Doron C.
Source :: Proceedings of the National Academy of Sciences of the United States of America; 8/23/2011, Vol. 108 Issue 34, p13885-13886, 2p
Publication Year :: 2011
Abstract: The article focuses on the use of bestatin-based activity-based probes (ABP), labeled PfA-M1 and Pf-LAP, in exploring the therapeutic potential of metallo-aminopeptidases (MAPs) in treating malaria. It notes that the probes produce varying chemotypes depending on the specificity of MAPs. Moreover, it implies that the inhibition of PfA-M1 in the Plasmodium falciparum, malaria-causing organism, causes elevation of the parasite's hemoglobin peptides.

Subjects :: BESTATIN
MALARIA treatment
AMINOPEPTIDASES
PLASMODIUM falciparum
PEPTIDES
HEMOGLOBINS

Language :: English
ISSN :: 00278424
Volume :: 108
Issue :: 34
Database :: Complementary Index
Journal :: Proceedings of the National Academy of Sciences of the United States of America
Publication Type :: Academic Journal
Accession number :: 65170571
Full Text :: https://doi.org/10.1073/pnas.1105601108

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