Exploring marine Lactobacillus and its protein for probiotic-based oral cancer therapy

Cancer is a life-threatening malignancy and one of the leading global causes of human mortality. New approaches are required for cancer therapy due to the unique properties of cancer cells and the side effects of chemotherapy. Probiotics have gained significant attention in the prevention and treatm...

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Published inInternational journal of biological macromolecules Vol. 254; no. Pt 1; p. 127652
Main Authors Vidya, Sankarapandian, Thiruneelakandan, Govindasamy, Krishnamoorthy, Rajapandiyan, Subbarayan, Shanthi, Maran, Balu Alagar Venmathi, Alshuniaber, Mohammad A., Gatasheh, Mansour K., Sunday, Bot Yakubu, Ahmad, Anis
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.01.2024
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Summary:Cancer is a life-threatening malignancy and one of the leading global causes of human mortality. New approaches are required for cancer therapy due to the unique properties of cancer cells and the side effects of chemotherapy. Probiotics have gained significant attention in the prevention and treatment of various diseases, including cancer. Therefore, the current study aimed to investigate the anti-cancer effects of probiotics, such as marine Lactobacillus species and their proteins. Five marine Lactobacillus species were isolated and identified from the Tamil Nadu Mangrove Pichavaram (TLMP) forest and named TLMP1, TLMP2, TLMP3, TLMP4, and TLMP5. The Lactobacillus isolates, and their proteins were administered to male golden Syrian hamsters. Tumor formation was effectively controlled in hamsters treated with crude Lactobacillus, extending their lifespan. Additionally, Lactobacillus proteins demonstrated an inhibitory effect on tumor formation in the treated group compared to the control. Molecular docking analysis revealed that Lactobacillus proteins interacted significantly with the cAMP-dependent protein kinase catalytic subunit alpha. Amino acid residues LYS791, MET793, ARG841, ARG842, and LEU844 were involved in active site binding and played a crucial role in inhibiting cAMP-dependent protein kinase.
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ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2023.127652