Selective and slow-binding inhibition of shikonin derivatives isolated from Lithospermum erythrorhizon on glycosyl hydrolase 33 and 34 sialidases = 지치로부터 분리한 쉬코닌 유도체들의 GH 33과 34에 대한 selective and slow-binding 저해 연구
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- Selective and slow-binding inhibition of shikonin derivatives isolated from Lithospermum erythrorhizon on glycosyl hydrolase 33 and 34 sialidases = 지치로부터 분리한 쉬코닌 유도체들의 GH 33과 34에 대한 selective and slow-binding 저해 연구
- J Y Kim; Hyung Jae Jung; Ji Young Park; Young Min Kim; Su-Jin Park; J K Cho; K H Park; Young Bae Ryu; Woo Song Lee
- Bibliographic Citation
- Bioorganic & Medicinal Chemistry, vol. 20, no. 5, pp. 1740-1748
- Publication Year
- Sialidases are enzymes that catalyze the hydrolysis of sialic acid residues from various glycoconjugates, which are widely found in a number of viral and microbial pathogens. In this study, we investigated the biological evaluation of isolated six shikonins (1-6) and three shikonofurans (7-9) from Lithospermum erythrorhizon. The nine isolated compounds 1-9 showed strong and selective inhibition of glycosyl hydrolase (GH) 33 and -34 sialidases activities. In GH33 bacterial-sialidase inhibition assay, the inhibitory activities against GH33 siadliase of all shikonofuran derivatives (7-9) were greater than shikonin derivatives (1-6). Shikonofuran E (8) exhibited the most potent inhibitory activity toward GH33 sialidases (IC 50 = 0.24 μM). Moreover, our detailed kinetic analysis of these species unveiled that they are all competitive and simple reversible slow-binding inhibitors. Otherwise, they showed different inhibitory capacities and kinetic modes to GH34 viral-sialidase activity. All the naphthoquinone derivatives (1-6) were of almost equal efficiency with IC 50 value of 40 μM and shikonofurans (7-9) did not show the significant inhibitory effect to GH34 sialidase. Kinetic analyses indicated that naphthoquinones acted via a noncompetitive mechanism.
- Glycosyl hydrolase; Lithospermum erythrorhizon; Shikonin; Shikonofuran; Sialidase
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- Jeonbuk Branch Institute > Functional Biomaterial Research Center > 1. Journal Articles
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