Synthetic Piperidine-substituted Chalcones as Potential Hits for α-Amylase Inhibitory and Antioxidant Activities - SUPPLEMENTARY MATERIAL.docx

Spectroscopic data (EIMS)

Spectroscopic data (NMR)

  

Table-S1: Kinetics data for α-amylase inhibitor

  

Figure-S1: Graph of compound 18; Lineweaver- Burk plot of reciprocal of rate of reaction (velocities) vs. reciprocal of the substrate (starch) in the different concentrations of inhibitor (0, 0.625, 1.25 and 2.5 µM). At the same time, Vmax and Km values were calculated from Lineweaver- Burk plot.

  

Figure-S2: Graph of compound 18; Dixon plot of reciprocal rate of reaction (velocities) vs. different inhibitor concentrations (0, 0.625, 1.25, and 2.5 µM). In contrast, the Ki value was calculated from the Dixon plot

  

Figure-S3: Dock pose of acarbose with a deviation.

  

Figure-S4: Intermolecular interactions performed by the inhibitors (A) 7, (B) 18, (C) 4, (D) 2, (E) 22, and (F) 17 in the α-amylase active site.

  

Table-S2: Dock score of the active compounds 2, 4, 7, 17, 18, and 22.