191403-66-4Relevant articles and documents
Synthesis of nature product kinsenoside analogues with anti-inflammatory activity
Song, Wei,Sun, Yong,Xu, Lintao,Sun, Yajing,Li, Tianlu,Peng, Peng,Lou, Hongxiang
supporting information, (2020/12/02)
Kinsenoside is the major bioactive component from herbal medicine with a broad range of pharmacological functions. Goodyeroside A, an epimer of kinsenoside, remains less explored. In this report we chemically synthesized kinsenoside, goodyeroside A and their analogues with glycan variation, chirality inversion at chiral center(s), and bioisosteric replacement of lactone with lactam. Among these compounds, goodyeroside A and its mannosyl counterpart demonstrated superior anti-inflammatory efficacy. Furthermore, goodyeroside A was found to suppresses inflammatory through inhibiting NF-κB signal pathway, effectively. Structure-activity relationship is also explored for further development of more promising kinsenoside analogues as drug candidates.
Gamma-lactam glycoside derivative, and synthesis method and application thereof
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, (2020/02/14)
The invention relates to a gamma-lactam glycoside derivative, and a synthesis method and application thereof. The structure of the formula I is shown as follows (please see the specification for the formula I), wherein R is selected from a beta-D-glucopyranose group, an alpha-D-glucopyranose group, a beta-D-galactopyranose group, an alpha-D-galactopyranose group, a beta-D-mannopyranose group, an alpha-D-mannopyranose grop, a beta-D-xylopyranose group, an alpha-D-xylopyranose group, a beta-L-pyran rhamnose group and an alpha-L-pyran rhamnose group, and the bond shown in the specification represents pointing to the page or the bond shown in the specification represents pointing out of the page.
Regio- and stereoselective biohydroxylations with a recombinant escherichia coli expressing P450pyr monooxygenase of sphingomonas Sp. HXN-200
Zhang, Wei,Tang, Weng Lin,Wang, Zunsheng,Li, Zhi
experimental part, p. 3380 - 3390 (2011/02/23)
A recombinant Escherichia coli expressing P450pyr monooxygenase of Sphingomonas sp. HXN-200 was developed as a useful biocatalyst for regio- and stereoselective hydroxylations, with no side reaction and easy cell growth. The resting E. coli cells showed an activity of 4.1 U/g cdw and 9.9 U/g cdw for the hydroxylation of N-benzylpyrrolidin-2-one 1 and N-benzyloxycarbonylpyrrolidine 3, respectively, being as active as the wide-type strain. Biohydroxylation of N-benzylpyrrolidin-2-one 1 with the resting cells gave (S)-N-benzyl-4- hydroxypyrrolidin-2-one 2 in >99% ee and 10.8 mM, a 2.6 times increase of product concentration in comparison with the wild-type strain. Biohydroxylation of N-tert-butoxycarbonylpiperidin-2-one 5, N-benzylpiperidine 7 and N-tert-butoxycarbonylazetidine 9 with the E. coli cells afforded the corresponding 4-hydroxypiperidin-2-one 6, 4-hydroxypiperidine 8, and 3-hydroxyazetidine 10 in 14 mM, 17 mM, and 21 mM, respectively. Moreover, hydroxylation of (-)-β-pinene 11 with the recombinant E. coli cells showed excellent regio- and stereoselectivity and gave (1R)-trans-pinocarveol 12 in 82% yield and 4.1 mM, which is over 200 times higher than that obtained with the best biocatalytic system known thus far. The recombinant strain was also able to hydroxylate other types of substrates with unique selectivity: biohydroxylation of norbornane 13 gave exo-norbornaeol 14, with exo/endo selectivity of 95%; tetralin 15 and 6-methoxytetralin 17 were hydroxylated at the non-activated 2-position, for the first time, with regioselectivities of 83-84%. Copyright