Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/29594
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dc.contributor.authorMaenpuen S.
dc.contributor.authorMee-udorn P.
dc.contributor.authorPinthong C.
dc.contributor.authorAthipornchai A.
dc.contributor.authorPhiwkaow K.
dc.contributor.authorWatchasit S.
dc.contributor.authorPimviriyakul P.
dc.contributor.authorRungrotmongkol T.
dc.contributor.authorTinikul R.
dc.contributor.authorLeartsakulpanich U.
dc.contributor.authorChitnumsub P.
dc.contributor.otherSrinakharinwirot University
dc.date.accessioned2023-11-15T02:09:16Z-
dc.date.available2023-11-15T02:09:16Z-
dc.date.issued2023
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85168797531&doi=10.1016%2fj.abb.2023.109712&partnerID=40&md5=f70cd82a7b68f2ebf9b112d64b75d2cb
dc.identifier.urihttps://ir.swu.ac.th/jspui/handle/123456789/29594-
dc.description.abstractMangiferin, a polyphenolic xanthone glycoside found in various botanical sources, including mango (Mangifera indica L.) leaves, can exhibit a variety of bioactivities. Although mangiferin has been reported to inhibit many targets, none of the studies have investigated the inhibition of serine hydroxymethyltransferase (SHMT), an attractive target for antimalarial and anticancer drugs. SHMT, one of the key enzymes in the deoxythymidylate synthesis cycle, catalyzes the reversible conversion of L-serine and (6S)-tetrahydrofolate (THF) into glycine and 5,10-methylene THF. Here, in vitro and in silico studies were used to probe how mangiferin isolated from mango leaves inhibits Plasmodium falciparum and human cytosolic SHMTs. The inhibition kinetics at pH 7.5 revealed that mangiferin is a competitive inhibitor against THF for enzymes from both organisms. Molecular docking and molecular dynamic (MD) simulations demonstrated the inhibitory effects of the deprotonated forms of mangiferin, specifically the C6–O- species and its resonance C9–O- species appearing at pH 7.5, combined with two docked poses, either a xanthone or glucose moiety, placed inside the THF-binding pocket. The MD analysis revealed that both C6–O- and its resonance-stabilized C9–O- species can favorably bind to SHMT in a similar fashion to THF, supporting the THF competitive inhibition of mangiferin. In addition, characterization of the proton dissociation equilibria of isolated mangiferin revealed that only three hydroxy groups of the xanthone moiety, C6–OH, C3–OH, and C7–OH, underwent varying degrees of deprotonation with pKa values of 6.38 ± 0.11, 8.21 ± 0.35, and 12.37 ± 0.30, respectively, while C1–OH remained protonated. Altogether, our findings demonstrate a new bioactivity of mangiferin and provide the basis for the future development of mangiferin as a potent antimalarial and anticancer drug. © 2023 Elsevier Inc.
dc.publisherAcademic Press Inc.
dc.subjectMangifera indica L.
dc.subjectMangiferin
dc.subjectPyridoxal-5′-phosphate enzymes
dc.subjectSerine hydroxymethyltransferase (SHMT)
dc.subjectSHMT inhibitor
dc.titleMangiferin is a new potential antimalarial and anticancer drug for targeting serine hydroxymethyltransferase
dc.typeArticle
dc.rights.holderScopus
dc.identifier.bibliograpycitationArchives of Biochemistry and Biophysics. Vol 745, No. (2023)
dc.identifier.doi10.1016/j.abb.2023.109712
Appears in Collections:Scopus 2023

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