Novel polycyclic meroterpenoids with protein tyrosine phosphatase 1B inhibitory activity isolated from desert-derived fungi Talaromyces sp. HMT-8
Abstract Seven previously undescribed polycyclic meroterpenoids talarines K–Q (1–7), along with five known ones (8–12), were isolated from desert-derived fungi Talaromyces sp. HMT-8. The structure of the novel compounds were elucidated using spectroscopic methods, including electronic circular dichr...
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| Format: | Article |
| Language: | English |
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SpringerOpen
2025-07-01
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| Series: | Natural Products and Bioprospecting |
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| Online Access: | https://doi.org/10.1007/s13659-025-00530-x |
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| author | Xin-yi Zhai Jin-jie Liu Cui-duan Wang Yi-fan Dou Jian-hua Lv Li-an Wang Jin-xiu Zhang Zhuang Li |
| author_facet | Xin-yi Zhai Jin-jie Liu Cui-duan Wang Yi-fan Dou Jian-hua Lv Li-an Wang Jin-xiu Zhang Zhuang Li |
| author_sort | Xin-yi Zhai |
| collection | DOAJ |
| description | Abstract Seven previously undescribed polycyclic meroterpenoids talarines K–Q (1–7), along with five known ones (8–12), were isolated from desert-derived fungi Talaromyces sp. HMT-8. The structure of the novel compounds were elucidated using spectroscopic methods, including electronic circular dichroism (ECD), HRESIMS and nuclear magnetic resonance (NMR) spectroscopy. Among the isolated meroterpenoids, compounds 3, 5, and 7 exhibited rare chlorine substitution patterns. Halogenation, particularly chlorination, is uncommon in natural meroterpenoids and implies the involvement of halogenase enzymes during biosynthesis. Compounds 1–12 were evaluated for their inhibitory activity against protein tyrosine phosphatase 1B (PTP1B). Compounds 1–4 and 12 exhibited inhibitory activity against PTP1B with IC₅₀ values ranging from 1.74 to 17.60 μM. Among them, compounds 2 and 12 displayed significant inhibitory effects with an IC₅₀ value of 1.74 and 3.03 μM, respectively. Furthermore, Molecular docking analysis revealed that compounds 2 and 12 bind tightly to the catalytic site of PTP1B, forming key hydrogen bonding and hydrophobic interactions. Enzyme kinetics studies further demonstrated that both compounds act as competitive inhibitor. Graphical Abstract |
| format | Article |
| id | doaj-art-eb45a554a18c4d8fb770fa0835a9e35a |
| institution | Kabale University |
| issn | 2192-2195 2192-2209 |
| language | English |
| publishDate | 2025-07-01 |
| publisher | SpringerOpen |
| record_format | Article |
| series | Natural Products and Bioprospecting |
| spelling | doaj-art-eb45a554a18c4d8fb770fa0835a9e35a2025-08-20T04:02:41ZengSpringerOpenNatural Products and Bioprospecting2192-21952192-22092025-07-0115111310.1007/s13659-025-00530-xNovel polycyclic meroterpenoids with protein tyrosine phosphatase 1B inhibitory activity isolated from desert-derived fungi Talaromyces sp. HMT-8Xin-yi Zhai0Jin-jie Liu1Cui-duan Wang2Yi-fan Dou3Jian-hua Lv4Li-an Wang5Jin-xiu Zhang6Zhuang Li7College of Life Sciences, Hebei Normal UniversitySchool of Land Science and Space Planning, Hebei GEO UniversityCollege of Life Sciences, Hebei Normal UniversityCollege of Life Sciences, Hebei Normal UniversityCollege of Life Sciences, Hebei Normal UniversityCollege of Life Sciences, Hebei Normal UniversityCollege of Life Sciences, Hebei Normal UniversityCollege of Life Sciences, Hebei Normal UniversityAbstract Seven previously undescribed polycyclic meroterpenoids talarines K–Q (1–7), along with five known ones (8–12), were isolated from desert-derived fungi Talaromyces sp. HMT-8. The structure of the novel compounds were elucidated using spectroscopic methods, including electronic circular dichroism (ECD), HRESIMS and nuclear magnetic resonance (NMR) spectroscopy. Among the isolated meroterpenoids, compounds 3, 5, and 7 exhibited rare chlorine substitution patterns. Halogenation, particularly chlorination, is uncommon in natural meroterpenoids and implies the involvement of halogenase enzymes during biosynthesis. Compounds 1–12 were evaluated for their inhibitory activity against protein tyrosine phosphatase 1B (PTP1B). Compounds 1–4 and 12 exhibited inhibitory activity against PTP1B with IC₅₀ values ranging from 1.74 to 17.60 μM. Among them, compounds 2 and 12 displayed significant inhibitory effects with an IC₅₀ value of 1.74 and 3.03 μM, respectively. Furthermore, Molecular docking analysis revealed that compounds 2 and 12 bind tightly to the catalytic site of PTP1B, forming key hydrogen bonding and hydrophobic interactions. Enzyme kinetics studies further demonstrated that both compounds act as competitive inhibitor. Graphical Abstracthttps://doi.org/10.1007/s13659-025-00530-xTalaromyces sp.Polycyclic meroterpenoidsPTP1BEnzyme kineticsMolecular docking |
| spellingShingle | Xin-yi Zhai Jin-jie Liu Cui-duan Wang Yi-fan Dou Jian-hua Lv Li-an Wang Jin-xiu Zhang Zhuang Li Novel polycyclic meroterpenoids with protein tyrosine phosphatase 1B inhibitory activity isolated from desert-derived fungi Talaromyces sp. HMT-8 Natural Products and Bioprospecting Talaromyces sp. Polycyclic meroterpenoids PTP1B Enzyme kinetics Molecular docking |
| title | Novel polycyclic meroterpenoids with protein tyrosine phosphatase 1B inhibitory activity isolated from desert-derived fungi Talaromyces sp. HMT-8 |
| title_full | Novel polycyclic meroterpenoids with protein tyrosine phosphatase 1B inhibitory activity isolated from desert-derived fungi Talaromyces sp. HMT-8 |
| title_fullStr | Novel polycyclic meroterpenoids with protein tyrosine phosphatase 1B inhibitory activity isolated from desert-derived fungi Talaromyces sp. HMT-8 |
| title_full_unstemmed | Novel polycyclic meroterpenoids with protein tyrosine phosphatase 1B inhibitory activity isolated from desert-derived fungi Talaromyces sp. HMT-8 |
| title_short | Novel polycyclic meroterpenoids with protein tyrosine phosphatase 1B inhibitory activity isolated from desert-derived fungi Talaromyces sp. HMT-8 |
| title_sort | novel polycyclic meroterpenoids with protein tyrosine phosphatase 1b inhibitory activity isolated from desert derived fungi talaromyces sp hmt 8 |
| topic | Talaromyces sp. Polycyclic meroterpenoids PTP1B Enzyme kinetics Molecular docking |
| url | https://doi.org/10.1007/s13659-025-00530-x |
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