α-Glucosidase-IN-120

α-Glucosidase-IN-120 (compound 10s) potently inhibits Saccharomyces cerevisiae α-glucosidase, with an IC₅₀ value of 12.01 μM, which is approximately 62.5 times more potent than Acarbose (HY-B0089)^[1].
α-Glucosidase-IN-120 (0-24 μM; 15 min) acts as a competitive inhibitor of Saccharomyces cerevisiae α-glucosidase, with a K_i value of 21 μM^[1].
α-Glucosidase-IN-120 (100 μM; 10 min) shows no inhibitory activity against bacterial α-amylase, demonstrating high selectivity for α-glucosidase^[1].
α-Glucosidase-IN-120 shows no cytotoxicity against MCF-7, HT-29, HDF and L929 cell lines at exposure for 48 h, with the maximum effective concentration reaching up to 100 μM^[1].
α-Glucosidase-IN-120 induces conformational changes in α-glucosidase from *Saccharomyces cerevisiae*, increases the ordered secondary structures of α-helices and β-turns, and eliminates the native β-sheets and random coil structures^[1].
α-Glucosidase-IN-120 (0-12 μM; 10 min) binds to *Saccharomyces cerevisiae* α-glucosidase with high affinity via static quenching, with a K_A of 7.6 × 10⁵ L mol^-1 and approximately 1 binding site at 25 °C, and hydrophobic interaction acts as the main driving force for this interaction^[1].
α-Glucosidase-IN-120 stably binds to the active site of Saccharomyces cerevisiae isomaltase, forming key hydrogen bonds and π-ion interactions associated with its potent α-glucosidase inhibitory activity^[1].
α-Glucosidase-IN-120 (200 ns) forms a stable and thermodynamically favorable complex with *Saccharomyces cerevisiae* isomaltase during the 200 ns MD simulation, a result supported by persistent hydrogen bonding and hydrophobic interactions, with an average MM-GBSA binding free energy ranging from −10 to −12 kcal/mol^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.