BACKGROUND: 'Phytonutrients' have been reported to exert an incredible impact on the healthcare system and offer medical benefits including the prevention or treatment of lifestyle-associated diseases. We chose one of the most common and important plant families, Musaceae, for our present study and explored its antidiabetic potential. RESULTS: Seeds of the edible fruits of Musa balbisianaColla. were investigated for their antidiabetic potential. After estimating the proximate composition, the seeds were extracted with various solvents and evaluated for antidiabetic potential in terms of the inhibition of digestive enzymes, antiglycation activity and in vitro glucose uptake. The acetone extract demonstrated the highest inhibition of -amylase and -glucosidase enzymes with IC 50 values of 36.67 ± 0.367 and 100.61 ± 0.707 g mL -1 , respectively. The extract also exhibited significant glycation inhibition with an IC 50 value of 86.48 ± 0.751 g mL -1 . Furthermore, a major phytochemical, apiforol, was isolated from the acetone extract for the first time, which demonstrated promising -glucosidase inhibition (IC 50 = 48.25 ± 0.255 mol L -1 ), antiglycation property (IC 50 = 114.23 ± 0.567 mol L -1 ) and enhanced glucose uptake in L6 myoblasts. In molecular docking studies, apiforol efficiently bonded to the active sites of -glucosidase enzyme 3A4A. CONCLUSIONS:As dietary intervention is one of the effective strategies for addressing diabetes, special attention is always given to natural food bio-actives or agro-products for better human health. The results of our study suggest that Musa balbisiana has significant potential as an ingredient in health food formulations by reducing postprandial hyperglycaemia.

Isoniazid (INH), one of the first-line drugs used for tuberculosis treatment, is a pro-drug which is activated by the intracellular KatG enzyme of Mycobacterium tuberculosis. The activated drug hinders cell wall biosynthesis by inhibiting InhA protein. INH resistant strains of M. tuberculosis usually have mutations in katG, inhA, ahpC, kasA, and ndh genes. However, INH resistant strains which do not have mutations in any of these genes are reported, suggesting that these strains may adopt some other mechanism to become resistant to INH. In the present study, we characterized Rv2170, a putative acetyltransferase in M. tuberculosis, to elucidate its role in inactivating isoniazid. The purified recombinant protein was able to catalyze the transfer of the acetyl group to INH from acetyl CoA. HPLC and LC-MS analyses showed that following acetylation by Rv2170, INH is broken down into isonicotinic acid and acetylhydrazine. Drug susceptibility assay and confocal analysis showed that M. smegmatis, which is susceptible to INH, is not inhibited by INH acetylated with Rv2170. Mutant proteins of Rv2170 failed to acetylate INH. Recombinant M. smegmatis and M. tuberculosis H37Ra overexpressing Rv2170 were found to be resistant to INH at minimum inhibitory concentrations that inhibited wildtype strains. Besides, intracellular M. tuberculosis H37Ra overexpressing Rv2170 survived better in macrophages when treated with INH. Our results strongly indicate that Rv2170 acetylates INH, and this could be one of the strategies adopted by at least some M. tuberculosis strains to overcome INH toxicity, although this needs to be tested in INH resistant clinical strains.

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