Novel bioactive peptides from ginkgo biloba seed protein and evaluation of their α-glucosidase inhibition activity
2022
Wang, Xiang | Deng, Yejun | Xie, Pujun | Liu, Lujie | Zhang, Caihong | Cheng, Jiang | Zhang, Yang | Liu, Yong | Huang, Lixin | Jiang, Jianxin
The inhibition of α-glucosidase activity has been recognized as an effective approach for treating type 2 diabetes mellitus (T2DM). In recent years, much emphasis has been placed on identifying peptides with α-glucosidase inhibitory activity and elucidating the mechanisms underlying their inhibitory effect in treating T2DM. This study aims to identify peptides with good α-glucosidase inhibitory activity from the hydrolysate of ginkgo biloba seed cake protein isolate (GCPI) using in silico screening. It was found that the hydrolysate from Alcalase exhibited the strongest inhibitory effect on α-glucosidase (IC₅₀ 12.94±0.37 mg/mL). Three novel peptides with α-glucosidase inhibitory activity, i.e., Leu-Ser-Met-Ser-Phe-Pro-Pro-Phe (LSMSFPPF), Val-Pro-Lys-Ile-Pro-Pro-Pro (VPKIPPP) and Met-Pro-Gly-Pro-Pro-Ser-Asp (MPGPPSD), were further identified from the hydrolysate of Alcalase by in silico screening. LSMSFPPF exhibited the strongest inhibitory activity (IC₅₀ 454.33±32.45 μM), followed by MPGPPSD (IC₅₀ 943.82±73.10 μM) and VPKIPPP (IC₅₀ 1446.81±66.98 μM). The pharmacophore model revealed that hydrogen bonds played a critical role in α-glucosidase inhibition.
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