Geranylation of Chalcones by a Fungal Aromatic Prenyltransferase.

Geranylated chalcones mainly exist in plants, and many of them have attracted attention because of their diverse pharmacological and biological activities. Herein, we report geranylation of eight chalcones by the aromatic prenyltransferase AtaPT. Ten new mono-geranylated enzyme products (-, , , , , and ) were obtained. Most of the products are -geranylated products with prenyl moieties at ring B. In comparison, plant aromatic prenyltransferases usually catalyze the geranylation at ring A. Therefore, AtaPT can be used complementarily for chalcone geranylation to increase the structural diversity of small molecules. In addition, seven compounds (, , , , , , and ) exhibited a potential inhibitory effect on α-glucosidase with the IC values ranging from 45.59 ± 3.48 to 82.85 ± 2.15 μg/mL. Among them, compound (45.59 ± 3.48 μg/mL) was the most potential α-glucosidase inhibitor, which is about seven times stronger than the positive control acarbose (IC = 346.63 ± 15.65 μg/mL).