@article{71897f8639304bd19a1c4e3f6cc62451,
title = "Improvement of both plasmepsin inhibitory activity and antimalarial activity by 2-aminoethylamino substitution",
abstract = "We attached 2-aminoethylamino groups to allophenylnorstatine-containing plasmepsin (Plm) inhibitors and investigated SAR of the methyl or ethyl substitutions on the amino groups. Unexpectedly, compounds 22 (KNI-10743) and 25 (KNI-10742) exhibited extremely potent Plm II inhibitory activities (K i <0.1 nM). Moreover, among our peptidomimetic Plm inhibitors, we identified the compounds with the highest antimalarial activity using a SYBR Green I-based fluorescence assay.",
keywords = "Allophenylnorstatine, Antimalarial drug, Aspartic protease, Hydoxymethylcarbonyl, Peptidomimetics, Plasmepsin inhibitor",
author = "Takuya Miura and Koushi Hidaka and Tsuyoshi Uemura and Keisuke Kashimoto and Yuto Hori and Yuko Kawasaki and Ruben, {Adam J.} and Ernesto Freire and Tooru Kimura and Yoshiaki Kiso",
note = "Funding Information: This research was supported in part by the {\textquoteleft}Academic Frontier{\textquoteright} Project for Private Universities, a matching fund subsidy from Ministry of Education, Culture, Sports, Science, and Technology of Japan ( MEXT ), and grants from MEXT. E.F. acknowledges grants from the National Institutes of Health ( GM57144 ) and the Johns Hopkins Malarial Research Institute . We gratefully acknowledge Mr. T. Hamada and Mr. H.-O. Kumada for mass spectrometry and Ms. M. Tadehara for synthetic assistance. We are grateful to Dr. J.-T. Nguyen for consultation and revision of the manuscript. We thank the Walter Reed Army Institute of Research for performing the antimalarial inhibition assays.",
year = "2010",
month = aug,
day = "15",
doi = "10.1016/j.bmcl.2010.06.099",
language = "English (US)",
volume = "20",
pages = "4836--4839",
journal = "Bioorganic and Medicinal Chemistry Letters",
issn = "0960-894X",
publisher = "Elsevier Limited",
number = "16",
}