The investigation of α-amylase inhibitory activity of selected Pinto bean peptides via preclinical study using AR42J cell

• Main Authors: Ying-Yuan Ngoh, Gee Jun Tye, Chee-Yuen Gan
• Format: Article
• Language: English
• Published: Elsevier 2017-08-01
• Series: Journal of Functional Foods
• Subjects: α-Amylase; AR42J cell; Diabetes treatment; Inhibitory activity; Pinto bean peptide
• Online Access: http://www.sciencedirect.com/science/article/pii/S1756464617303559

The current work investigated the α-amylase inhibitory activity of five selected Pinto bean peptides (PBPs) using AR42J cell. The objectives were: (a) to prove the potential of PBPs as α-amylase inhibitor in living cells, and (b) to investigate the inhibition mode of PBPs. Results showed that PBP9 obtained the lowest IC50 value of 0.31 mM followed by PBP7 (5.92 mM), PBP1 (6.08 mM), PBP6 (6.14 mM) and PBP3 (6.64 mM). In the MTT assay, all PBP showed a dose-dependent trend, whereby lower concentration of PBP demonstrated a higher cell viability. By using PBP concentrations of 0.33–8.3 mM, Michaelis-Menten kinetic parameters and Lineweaver-Burk plots revealed that Km and Vmax values were ranged from 38.52–794.38 mM and 0.72–1.15 mM/min, respectively, resulting in uncompetitive (PBP3, PBP6 and PBP7) and unusual (PBP1 and PBP9) α-amylase inhibition modes. It was suggested that PBP could be considered as new agents for the diabetes treatment.