Abstract
Understanding the interaction of (-)-epigallocatechin-3-gallate (EGCG) and lipase is important for understanding EGCG's inhibition of lipase. In this paper, the interaction of EGCG and porcine lipase was characterized by fluorescence spectroscopy, circular dichroism (CD), isothermal titration calorimetry, and molecular docking. EGCG might act as a noncompetitive pancreatic lipase inhibiter. EGCG bound to lipase with affinity of K(a) = 2.70 × 10⁴ L mol⁻¹. Thermodynamic features suggested that the interaction process was spontaneous, with hydrogen bonds and electrostatic force perhaps primarily responsible for the interaction, with 1:1 interaction of lipase and EGCG. CD studies indicated conformation change of lipase on binding to EGCG. Furthermore, docking results supported experimental findings and revealed hydrogen-bonding interaction with Val21, Glu188, and Glu220. This noncovalent bonding between EGCG and lipase alters the molecular conformation of lipase, which decreases the enzyme catalytic activity. This study will help further understand the antiobesity mechanisms of green tea.
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