Design, synthesis, α-glucosidase inhibitory activity, and molecular docking of novel pyrazolyl-porphyrin hybrids as potential antidiabetic agents

A novel series of A₂B₂ and A₄ type porphyrin derivatives bearing pyrazole moieties was efficiently synthesized and structurally characterized. These pyrazolyl-porphyrins were evaluated for their α-glucosidase inhibitory activity using Saccharomyces cerevisiae α-glucosidase as the target enzyme. In vitro enzyme assays and kinetic studies revealed that compounds 6c, 7b, and 6d exhibited inhibitory effects comparable to the standard drug Acarbose. Notably, compound 6c demonstrated the highest potency, with an IC₅₀ value of (31.36 μM), closely matching that of Acarbose (31.69 μM) under identical experimental conditions. In silico molecular docking studies further supported the biological data, showing that compound 6c interacts with key residues within the enzyme's active site in a binding mode similar to Acarbose. These findings suggest that pyrazolyl-porphyrin hybrids, particularly compound 6c, hold promise as potential α-glucosidase inhibitors for the development of antidiabetic agents.

Enzyme kinetics; Molecular docking studies; Pyrazolyl–porphyrin derivatives; α-Glucosidase inhibition.