Synthesis and structure-activity relationships of phosphonic arginine mimetics as inhibitors of the M1 and M17 aminopeptidases from plasmodium falciparum

Kannan Sivaraman, K; Paiardini, A; Sieńczyk, M; Ruggeri, C; Oellig, CA; Dalton, JP; Scammells, PJ; Drag, M; McGowan, S

Synthesis and structure-activity relationships of phosphonic arginine mimetics as inhibitors of the M1 and M17 aminopeptidases from plasmodium falciparum

Kannan Sivaraman, K Paiardini, A Sieńczyk, M Ruggeri, C Oellig, CA Dalton, JP Scammells, PJ Drag, M McGowan, S

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Publication Type:: Journal Article
Citation:: Journal of Medicinal Chemistry, 2013, 56 (12), pp. 5213 - 5217
Issue Date:: 2013-06-27

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Field	Value	Language
dc.contributor.author	Kannan Sivaraman, K	en_US
dc.contributor.author	Paiardini, A	en_US
dc.contributor.author	Sieńczyk, M	en_US
dc.contributor.author	Ruggeri, C	en_US
dc.contributor.author	Oellig, CA	en_US
dc.contributor.author	Dalton, JP	en_US
dc.contributor.author	Scammells, PJ	en_US
dc.contributor.author	Drag, M	en_US
dc.contributor.author	McGowan, S	en_US
dc.date.issued	2013-06-27	en_US
dc.identifier.citation	Journal of Medicinal Chemistry, 2013, 56 (12), pp. 5213 - 5217	en_US
dc.identifier.issn	0022-2623	en_US
dc.identifier.uri	http://hdl.handle.net/10453/23944
dc.description.abstract	The malaria parasite Plasmodium falciparum employs two metallo- aminopeptidases, PfA-M1 and PfA-M17, which are essential for parasite survival. Compounds that inhibit the activity of either enzyme represent leads for the development of new antimalarial drugs. Here we report the synthesis and structure-activity relationships of a small library of phosphonic acid arginine mimetics that probe the S1 pocket of both enzymes and map the necessary interactions that would be important for a dual inhibitor. © 2013 American Chemical Society.	en_US
dc.relation.ispartof	Journal of Medicinal Chemistry	en_US
dc.relation.isbasedon	10.1021/jm4005972	en_US
dc.subject.classification	Medicinal & Biomolecular Chemistry	en_US
dc.subject.mesh	Plasmodium falciparum	en_US
dc.subject.mesh	Phosphorous Acids	en_US
dc.subject.mesh	Antigens, CD13	en_US
dc.subject.mesh	Arginine	en_US
dc.subject.mesh	Enzyme Inhibitors	en_US
dc.subject.mesh	Catalytic Domain	en_US
dc.subject.mesh	Structure-Activity Relationship	en_US
dc.subject.mesh	Models, Molecular	en_US
dc.subject.mesh	Biomimetic Materials	en_US
dc.subject.mesh	Chemistry Techniques, Synthetic	en_US
dc.subject.mesh	CD13 Antigens	en_US
dc.title	Synthesis and structure-activity relationships of phosphonic arginine mimetics as inhibitors of the M1 and M17 aminopeptidases from plasmodium falciparum	en_US
dc.type	Journal Article
utslib.citation.volume	12	en_US
utslib.citation.volume	56	en_US
utslib.for	0304 Medicinal and Biomolecular Chemistry	en_US
utslib.for	1115 Pharmacology and Pharmaceutical Sciences	en_US
utslib.for	0305 Organic Chemistry	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
utslib.copyright.status	closed_access
pubs.issue	12	en_US
pubs.publication-status	Published	en_US
pubs.volume	56	en_US

Abstract:

The malaria parasite Plasmodium falciparum employs two metallo- aminopeptidases, PfA-M1 and PfA-M17, which are essential for parasite survival. Compounds that inhibit the activity of either enzyme represent leads for the development of new antimalarial drugs. Here we report the synthesis and structure-activity relationships of a small library of phosphonic acid arginine mimetics that probe the S1 pocket of both enzymes and map the necessary interactions that would be important for a dual inhibitor. © 2013 American Chemical Society.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/23944