Please use this identifier to cite or link to this item: https://doi.org/10.1038/ja.2012.123
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dc.titleIsolation and synthesis of falcitidin, a novel myxobacterial-derived acyltetrapeptide with activity against the malaria target falcipain-2
dc.contributor.authorSomanadhan, B.
dc.contributor.authorKotturi, S.R.
dc.contributor.authorYan Leong, C.
dc.contributor.authorGlover, R.P.
dc.contributor.authorHuang, Y.
dc.contributor.authorFlotow, H.
dc.contributor.authorBuss, A.D.
dc.contributor.authorLear, M.J.
dc.contributor.authorButler, M.S.
dc.date.accessioned2014-06-23T05:42:31Z
dc.date.available2014-06-23T05:42:31Z
dc.date.issued2013-05
dc.identifier.citationSomanadhan, B., Kotturi, S.R., Yan Leong, C., Glover, R.P., Huang, Y., Flotow, H., Buss, A.D., Lear, M.J., Butler, M.S. (2013-05). Isolation and synthesis of falcitidin, a novel myxobacterial-derived acyltetrapeptide with activity against the malaria target falcipain-2. Journal of Antibiotics 66 (5) : 259-264. ScholarBank@NUS Repository. https://doi.org/10.1038/ja.2012.123
dc.identifier.issn00218820
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/76417
dc.description.abstractA 384-well microtitre plate fluorescence cleavage assay was developed to identify inhibitors of the cysteine protease falcipain-2, an important antimalarial drug target. Bioassay-guided isolation of a MeOH extract from a myxobacterium Chitinophaga sp. Y23 isolated from soil collected in Singapore, led to the identification of a new acyltetrapeptide, falcitidin (1), which displayed an IC 50 value of 6 μM against falcipain-2. The planar structure of 1 was secured by NMR and MS/MS analysis. Attempts to isolate further material for biological testing were hampered by inconsistent production and by a low yield (<100 μg l -1). The absolute configuration of 1 was determined by Marfey's analysis and the structure was confirmed through total synthesis as isovaleric acid-D-His-L-Ile-L-Val-L-Pro-NH 2. Falcitidin (1) is the first member of a new class of falcipain-2 inhibitors and, unlike other peptide-based inhibitors, does not contain reactive groups that irreversibly bind to active cysteine sites. © 2013 Japan Antibiotics Research Association All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1038/ja.2012.123
dc.sourceScopus
dc.subjectChitinophaga
dc.subjectFalcipain
dc.subjectFalcitidin
dc.subjectMalaria
dc.subjectMyxobacteria
dc.subjectTetrapeptide
dc.typeArticle
dc.contributor.departmentCHEMISTRY
dc.description.doi10.1038/ja.2012.123
dc.description.sourcetitleJournal of Antibiotics
dc.description.volume66
dc.description.issue5
dc.description.page259-264
dc.description.codenJANTA
dc.identifier.isiut000319503900002
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