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Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase.

ABSTRACT: The parasite Plasmodium vivax is the most widely distributed cause of recurring malaria. N-Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both Plasmodium vivax and Plasmodium falciparum N-myristoyltransferase (NMT).

SUBMITTER: Goncalves V

PROVIDER: S-EPMC5463734 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature

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Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase.

Goncalves Victor V Brannigan James A JA Laporte Alice A Bell Andrew S AS Roberts Shirley M SM Wilkinson Anthony J AJ Leatherbarrow Robin J RJ Tate Edward W EW

MedChemComm 20161111 1

The parasite Plasmodium vivax is the most widely distributed cause of recurring malaria. N-Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both Plasmodium vivax and Plasmodium falcip ...[more]

PMID: 28626547

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