The mechanism of chlorogenic acid inhibits lipid oxidation: An investigation using multi-spectroscopic methods and molecular docking

Abstract

Endogenous lipase and lipoxygenase play important roles in accelerating lipid oxidation.Polyphenols are a series of commonly used chemicals for preserving fish and seafood products, due to their positive inhibitory effects on lipid oxidation. However, the mechanism involved is still unknown. The inhibitory effects of chlorogenic acid (CGA) on lipase and lipoxygenase were investigated and explored with multi-spectroscopic and molecular docking approaches. Results showed that CGA could inhibit the activities of lipase and lipoxygenase with concentration increased in a highly dose-dependent manner. CGA quenched intrinsic fluorescence intensities of enzymes by static quenching and binding with CGA which led to changes in 3D structures of enzymes. Results of the molecular docking confirmed binding modes, binding sites and major interaction forces between CGA and enzymes, which reduced the corresponding activity. Thus, this study could provide basic mechanisms of the inhibitory effects of polyphenols on lipid oxidation during food preservation.

Binding mechanism of lipase with Lentinus edodes mycelia polysaccharide by multi‐spectroscopic methods

“…Δ G° < 0 manifested that this binding was spontaneous 44 . Values of Δ H° and Δ S° were −97.57 kJ/mol and −241.23 J/mol K, indicating that the binding between chlorogenic acid and lipase was also mainly attributed to hydrogen bond and van der Waals forces 23 …”

“…It determined that the quenching mechanism was static quenching 33 . The quenching mechanism Ligupurpuroside B, chlorogenic acid binding with lipase were also static quenching 23,38 …”

“…1 cm quartz colorimetric dish with light transmittance from all sides was used. The fluorescence intensity was rectified with the following equation 23 : where F cor denotes the fluorescence intensity obtained after correction, F obs denotes the observed fluorescence intensity. A ex denotes the ultraviolet absorption value of LMP at excitation wavelengths, A em denotes the ultraviolet absorption value at emission wavelengths.…”

Effects of temperature and pH on the structure of a metalloprotease from Lactobacillus fermentumR6 isolated from Harbin dry sausages and molecular docking between protease and meat protein

“…Moreover, there were hydrophobic interactions between 15 residues of the protease, such as Val‐229, Ala‐234, His‐230, Ile‐242, Asn‐376, Asn‐376, Thr‐362, Glu‐209, Asp‐363, Glu‐180, Val‐ 277, Pro‐124, Met‐384, Thr‐119, Phe‐123, Phe‐388 and Gln‐243, and nine residues of myosin light chain, such as His‐119, Phe‐110, Lys‐12, Ser‐3, Met‐1, Gln‐16, Pro‐15, Leu‐126 and Gly‐131. Thus, hydrogen bonds and hydrophobic interactions are the major interactive forces that promote the binding of protease and myosin light chain and also can accelerate the catalysis effect of protease on substrate 49 . In addition, related studies have shown that protease may cleave the substrate protein correctly through the hydrogen bond between the protease and substrate 50 .…”

Potential of phenolic compounds in Ligustrum robustum (Rxob.) Blume as antioxidant and lipase inhibitors: Multi‐spectroscopic methods and molecular docking

“…The bound conformations and binding sites of ligand and protein were further analyzed based on the calculation results (Cao et al, 2020).…”