Plasmodium falciparum neutral aminopeptidases: new targets for anti-malarials

No Thumbnail Available
File version
Author(s)
Skinner-Adams, Tina S
Stack, Colin M
Trenholme, Katharine R
Brown, Chris L
Grembecka, Jolanta
Lowther, Jonathan
Mucha, Artur
Drag, Marcin
Kafarski, Pawel
McGowan, Sheena
Whisstock, James C
Gardiner, Donald L
Dalton, John P
Griffith University Author(s)
Primary Supervisor
Other Supervisors
Editor(s)

Sara Cullinan

Date
2010
Size
File type(s)
Location
License
Abstract

The neutral aminopeptidases M1 alanyl aminopeptidase (PfM1AAP) and M17 leucine aminopeptidase (PfM17LAP) of the humanmalaria parasite Plasmodiumfalciparumare targets for the development of novel anti-malarial drugs. Although the functions of these enzymes remain unknown, they are believed to act in the terminal stages of haemoglobin degradation, generating amino acids essential for parasite growth and development. Inhibitors of both enzymes are lethal to P. falciparum in culture and kill the murine malaria P. chabaudi in vivo. Recent biochemical, structural and functional studies provide the substrate specificity and mechanistic binding data needed to guide the development of more potent antimalarial drugs. Together with biological studies, these data form the rationale for choosing PfM1AAP and PfM17LAP as targets for anti-malarial development.

Journal Title

Trends in Biochemical Sciences

Conference Title
Book Title
Edition
Volume

35

Issue

1

Thesis Type
Degree Program
School
Publisher link
Patent number
Funder(s)
Grant identifier(s)
Rights Statement
Rights Statement
Item Access Status
Note
Access the data
Related item(s)
Subject

Chemical sciences

Medicinal and biomolecular chemistry not elsewhere classified

Biological sciences

Biomedical and clinical sciences

Persistent link to this record
Citation
Collections