Journal of complementary & integrative medicine · 2025
Exploring the anticancer potential of Jerantinine A from Tabernaemontana coronaria against prostate, breast, and ovarian cancers: a computational approach.
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Kannappan Poornima, Kaniyur Chandrasekaran Meenakshi, Vani Raju Manikandan, Gopalakrishnan Shankari, Dhamodharan Prabhu, Muthaiyan Ahalliya Rathi, Palanisamy Chella Perumal, Raju Balaji, Velliyur Kanniappan Gopalakrishnan
Аннотация
OBJECTIVES: Cancer remains a significant global health challenge, with prostate, breast, and ovarian cancers ranking among the leading causes of morbidity and mortality. Natural products, particularly those derived from medicinal plants, have gained attention for their potential in alternative cancer therapies. The main objective of the study was an isolation and characterization of Jerantinine A, a bioactive alkaloid from Tabernaemontana coronaria, and its interactions with key protein targets involved in cancer progression.
METHODS: Jerantinine A was isolated through column chromatography and characterized using spectroscopic techniques, including UV-visible spectroscopy, FTIR, and NMR. Molecular docking studies were performed to assess its binding affinities with six critical protein targets: PTEN and androgen receptor for prostate cancer, CXCR4 and HER2 for ovarian cancer, and CDK1 and NEK2 for breast cancer.
RESULTS: Molecular docking analyses revealed that Jerantinine A exhibits strong binding affinities with all six protein targets, suggesting its potential to inhibit cancer cell proliferation by interfering with key signaling pathways.
CONCLUSIONS: These findings underscore the therapeutic potential of T. coronaria, particularly through Jerantinine A, as a promising candidate for cancer treatment. By targeting pivotal proteins associated with prostate, breast, and ovarian cancers, Jerantinine A offers a foundation for further research and development as a novel anti-cancer agent.
METHODS: Jerantinine A was isolated through column chromatography and characterized using spectroscopic techniques, including UV-visible spectroscopy, FTIR, and NMR. Molecular docking studies were performed to assess its binding affinities with six critical protein targets: PTEN and androgen receptor for prostate cancer, CXCR4 and HER2 for ovarian cancer, and CDK1 and NEK2 for breast cancer.
RESULTS: Molecular docking analyses revealed that Jerantinine A exhibits strong binding affinities with all six protein targets, suggesting its potential to inhibit cancer cell proliferation by interfering with key signaling pathways.
CONCLUSIONS: These findings underscore the therapeutic potential of T. coronaria, particularly through Jerantinine A, as a promising candidate for cancer treatment. By targeting pivotal proteins associated with prostate, breast, and ovarian cancers, Jerantinine A offers a foundation for further research and development as a novel anti-cancer agent.