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  • Open Access

    ARTICLE

    Three New Hydroxytetradecenals from Amomum tsao-ko with Protein Tyrosine Phosphatase 1B and Glycogen Phosphorylase Inhibitory Activity

    Xiaolu Qin1,3, Xinyu Li1,3, Yi Yang2, Mei Huang2, Shengli Wu1, Pianchou Gongpan1, Lianzhang Wu2, Juncai He2, Changan Geng1,3,*

    Phyton-International Journal of Experimental Botany, Vol.93, No.5, pp. 875-883, 2024, DOI:10.32604/phyton.2024.048192

    Abstract The fruits of Amomum tsao-ko (Cao-Guo) were documented in Chinese Pharmacopoeia for the treatment of abdominal pain, vomiting, and plague. In our previous study, a series of diarylheptanes and flavonoids with α-glucosidase and protein tyrosine phosphatase 1B (PTP1B) inhibitory activity have been reported from the middle-polarity part of A. tsao-ko, whereas the antidiabetic potency of the low-polarity constituents is still unclear. In this study, three new hydroxytetradecenals, (2E, 4E, 8Z, 11Z)-6R-hydroxytetradeca-2,4,8,11-tetraenal (1), (2E, 4E, 8Z)-6R-hydroxytetradeca-2,4,8-trienal (2) and (2E, 4E)-6R-hydroxytetradeca-2,4-dienal (3) were obtained from the volatile oils of A. tsao-ko. The structures of compounds 1–3 were determined using spectroscopic data involving 1D and 2D nuclear magnetic More >

  • Open Access

    ARTICLE

    POM analysis and computational interactions of 8-hydroxydiospyrin inside active site of protein tyrosine phosphatase 1B

    SAUD BAWAZER1, ASGHAR KHAN2, ABDUR RAUF3,*, TAIBI BEN HADDA4, YAHYA S. AL-AWTHAN5,6, OMAR BAHATTAB5, UMER RASHID7, INAMULLAH KHAN8, MUHAMMAD ASIF NAWAZ9, MD SAHAB UDDIN10,11, OLATUNDE AHMED12, MOHAMMAD ALI SHARIATI13

    BIOCELL, Vol.45, No.3, pp. 751-759, 2021, DOI:10.32604/biocell.2021.014004

    Abstract Protein tyrosine phosphatase 1B (PTP1B) inhibition is considered as a potential therapeutic for the treatment of cancer, type 2 diabetes, and obesity. In our present work, we investigated the anti-diabetic potential of 8-hydroxydiospyrin (8-HDN) from D. lotus against the PTP1B enzyme. It showed significant inhibitory activity of PTP1B with an IC50 value of 18.37 ± 0.02 μM. A detailed molecular docking study was carried out to analyze the binding orientation, binding energy, and mechanism of inhibition. A comparative investigation of 8-HDN in the catalytic, as well as the allosteric site of PTP1B, was performed. Binding energy data More >

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