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The present study investigated the antidiabetic properties of the extracts and fractions from leaves and stem bark of M. glabra based on dipeptidyl peptidase-4 (DPP-4) and α-Amylase inhibitory activity assays. The chloroform extract of the leaves was found to be most active towards inhibition of DPP-4 and α-Amylase with IC 50 of 169.40 μg/mL and 303.64 μg/mL, respectively. Bioassay-guided fractionation of the leaves' chloroform extract revealed fraction 4 (CF4) as the most active fraction (DPP-4 IC 50 : 128.35 μg/mL; α-Amylase IC 50 : 170.19 μg/mL). LC-MS/MS investigation of CF4 led to the identification of trans-decursidinol ( 1 ), swermirin ( 2 ), methyl 3,4,5-trimethoxycinnamate ( 3 ), renifolin ( 4 ), 4',5,6,7-tetramethoxy-flavone ( 5 ), isorhamnetin ( 6 ), quercetagetin-3,4'-dimethyl ether ( 7 ), 5,3',4'-trihydroxy-6,7-dimethoxy-flavone ( 8 ), and 2-methoxy-5-acetoxy-fruranogermacr-1(10)-en-6-one ( 9 ) as the major components. The computational study suggested that ( 8 ) and ( 7 ) were the most potent DPP-4 and α-Amylase inhibitors based on their lower binding affinities and extensive interactions with critical amino acid residues of the respective enzymes. The binding affinity of ( 8 ) with DPP-4 (-8.1 kcal/mol) was comparable to that of sitagliptin (-8.6 kcal/mol) while the binding affinity of ( 7 ) with α-Amylase (-8.6 kcal/mol) was better than acarbose (-6.9 kcal/mol). These findings highlight the phytochemical profile and potential antidiabetic compounds from M. glabra that may work as an alternative treatment for diabetes.

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Identification of Dipeptidyl Peptidase-4 and α-Amylase Inhibitors from Melicope glabra (Blume) T. G. Hartley (Rutaceae) Using Liquid Chromatography Tandem Mass Spectrometry, In Vitro and In Silico Methods