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  1. Maulana AF, Aisyah RN, Sriwidodo S, Maksum IP, Rukayadi Y
    Curr Drug Deliv, 2026;23(8):984-995.
    PMID: 42958850 DOI: 10.2174/0115672018422136260130000617
    INTRODUCTION: Type 2 diabetes mellitus represents a growing global health burden, with current α-glucosidase inhibitors such as acarbose and miglitol demonstrating limited efficacy and notable gastrointestinal side effects. α-Mangostin, a bioactive compound from mangosteen peel, shows promise as a natural α-glucosidase inhibitor but suffers from poor aqueous solubility. This study aimed to enhance the solubility and enzyme inhibitory activity of mangosteen peel extract through amorphous solid dispersion using two manufacturing approaches: solvent evaporation and fluidized bed drying.

    METHODS: Mangosteen peel extract was formulated into amorphous solid dispersions using polyvinylpyrrolidone K30 at a 1:3 polymer ratio via solvent evaporation and fluidized bed drying methods. Solubility enhancement was evaluated under standardized conditions, and α-glucosidase inhibitory activity was assessed through IC50 determination. Comparative analysis against acarbose and quercetin standards was performed.

    RESULTS: Solvent evaporation achieved 2.1-fold solubility enhancement, while fluidized bed drying yielded 1.8-fold improvement. The mangosteen peel extract demonstrated superior α-glucosidase inhibition (IC50 = 20.13 ± 0.02 μg/mL) compared to acarbose (IC50 = 379.75 ± 0.57 μg/mL) but remained less potent than quercetin (IC50 = 2.97 ± 0.05 μg/mL). When normalized to equivalent α- mangostin concentrations, fluidized bed drying preserved inhibitory activity more effectively (IC50 = 112.87 ± 0.06 μg/mL) than solvent evaporation (IC50 = 1238.48 ± 0.51 μg/mL).

    DISCUSSION: The manufacturing method significantly influenced both solubility and biological activity. Solvent evaporation maximized solubility enhancement but compromised enzyme inhibitory potency, whereas fluidized bed drying maintained superior inhibitory activity despite moderate solubility improvement. This trade-off suggests that formulation strategy selection should prioritize the desired therapeutic outcome.

    CONCLUSION: Amorphous solid dispersion successfully enhanced both solubility and α-glucosidase inhibitory activity of mangosteen peel extract. Fluidized bed drying represents the optimal manufacturing approach for preserving enzyme inhibition while achieving meaningful solubility enhancement, positioning α-mangostin as a promising candidate for natural antidiabetic drug development.

    Matched MeSH terms: Acarbose/chemistry
  2. Mok SC, Teh AH, Saito JA, Najimudin N, Alam M
    Enzyme Microb Technol, 2013 Jun 10;53(1):46-54.
    PMID: 23683704 DOI: 10.1016/j.enzmictec.2013.03.009
    A truncated form of an α-amylase, GTA, from thermophilic Geobacillus thermoleovorans CCB_US3_UF5 was biochemically and structurally characterized. The recombinant GTA, which lacked both the N- and C-terminal transmembrane regions, functioned optimally at 70°C and pH 6.0. While enzyme activity was not enhanced by the addition of CaCl2, GTA's thermostability was significantly improved in the presence of CaCl2. The structure, in complex with an acarbose-derived pseudo-hexasaccharide, consists of the typical three domains and binds one Ca(2+) ion. This Ca(2+) ion was strongly bound and not chelated by EDTA. A predicted second Ca(2+)-binding site, however, was disordered. With limited subsites, two novel substrate-binding residues, Y147 and Y182, may help increase substrate affinity. No distinct starch-binding domain is present, although two regions rich in aromatic residues have been observed. GTA, with a smaller domain B and several shorter loops compared to other α-amylases, has one of the most compact α-amylase folds that may contribute greatly to its tight Ca(2+) binding and thermostability.
    Matched MeSH terms: Acarbose/chemistry
  3. Zawawi NK, Taha M, Ahmat N, Wadood A, Ismail NH, Rahim F, et al.
    Bioorg Chem, 2016 Feb;64:29-36.
    PMID: 26637946 DOI: 10.1016/j.bioorg.2015.11.006
    Newly synthesized benzimidazole hydrazone derivatives 1-26 were evaluated for their α-glucosidase inhibitory activity. Compounds 1-26 exhibited varying degrees of yeast α-glucosidase inhibitory activity with IC50 values between 8.40 ± 0.76 and 179.71 ± 1.11 μM when compared with standard acarbose. In this assay, seven compounds that showed highest inhibitory effects than the rest of benzimidazole series were identified. All the synthesized compounds were characterized by different spectroscopic methods adequately. We further evaluated the interaction of the active compounds with enzyme with the help of docking studies.
    Matched MeSH terms: Acarbose/chemistry
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