Journal article

Peptide Inhibitors of the Malaria Surface Protein, Apical Membrane Antigen 1: Identification of Key Binding Residues

Erinna F Lee, Shenggen Yao, Jennifer K Sabo, W Douglas Fairlie, Rachel A Stevenson, Karen S Harris, Robin F Anders, Michael Foley, Raymond S Norton

BIOPOLYMERS | WILEY | Published : 2011

Abstract

Apical membrane antigen 1 (AMA1) is essential for malaria parasite invasion of erythrocytes and is therefore an attractive target for drug development. Peptides that bind AMA1 have been identified from random peptide libraries expressed on the surface of phage. Of these, R1, which binds to a hydrophobic ligand binding site on AMA1, was a particularly potent inhibitor of parasite invasion of erythrocytes in vitro. The solution structure of R1 contains a turn-like conformation between residues 5-10. Here the importance of residues in this turn-like structure for binding to AMA1 was examined by site-directed mutagenesis and NMR spectroscopy. The peptide was expressed as a fusion protein followi..

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University of Melbourne Researchers

Grants

Awarded by Australian National Health and Medical Research Council of Australia


Awarded by IRIISS


Awarded by National Institutes of Health


Awarded by NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES


Funding Acknowledgements

Contract grant sponsor: Australian National Health and Medical Research Council of AustraliaContract grant number: 305525Contract grant sponsor: IRIISSContract grant number: 361646Contract grant sponsor: National Institutes of HealthContract grant number: NIH RO1AI59229Contract grant sponsor: Victorian State Government OIS