Journal article
Rapid optimization of a peptide inhibitor of malaria parasite invasion by comprehensive N-methyl scanning
KS Harris, JL Casey, AM Coley, JA Karas, JK Sabo, YY Tan, O Dolezal, RS Norton, AB Hughes, D Scanlon, M Foley
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2009
Abstract
Apical membrane antigen 1 (AMA1) of the malaria parasite Plasmodium falciparum has been implicated in the invasion of host erythrocytes and is an important vaccine candidate. We have previously described a 20-residue peptide, R1, that binds to AMA1 and subsequently blocks parasite invasion. Because this peptide appears to target a site critical for AMA1 function, it represents an important lead compound for anti-malarial drug development. However, the effectiveness of this peptide inhibitor was limited to a subset of parasite isolates, indicating a requirement for broader strain specificity. Furthermore, a barrier to the utility of any peptide as a potential therapeutic is its susceptibility..
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Awarded by National Institute of Allergy and Infectious Diseases
Funding Acknowledgements
This work was supported, in whole or in part, by National Institutes of Health Grant NIH RO1AI59229. This work was also supported by the National Health and Medical Research Council of Australia. The authors declare that they have no competing financial interests. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.