Binding mechanism of lipase to Ligupurpuroside B extracted from Ku-Ding tea as studied by multi-spectroscopic and molecular docking methods

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

“…The K b values of LMP were (2.44 ± 0.08) × 10 5 (290 K), (1.18 ± 0.04) × 10 5 (298 K), (0.87 ± 0.03 K) × 10 5 (304) and (0.53 ± 0.01) × 10 5 (310 K) L/mol. These results showed that the binding LMP and lipase had strong stability 38 . At 298 K, the binding site of hesperidin was 1.2974 and the K b was 8.13 × 10 5 L/mol, indicating that hesperidin also had only one binding site and had good stability in forming the combine with lipase 21 …”

“…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 …”

“…Peak 2 was the peak of the lipase polypeptide chain backbone on account of π → π* transition 26 . Peak a was the Rayleigh scattering peak 38 . Uncombined lipase was shown in Figure.…”

Isolation and Identification of Lipid-Lowering Peptides from Sacha Inchi Meal

“…In Table S2 , as the temperature increases from 298 K to 310 K, the quenching constant Ksv of pancreatic lipase by NV-7 decreased from 4.62 × 103 L/mol to 3.27 × 10 3 L/mol, Kq decreased from 4.62 × 10 11 mol/(L·s) to 3.27 × 10 11 mol/(L·s), both greater than the maximum fluorescence dynamic quenching rate constant 2 × 10 10 mol/(L·s), and the quenching constant Ksv gradually decreased with the increase of temperature, indicating that the increase of temperature was not helpful to the combination of NV-7 and pancreatic lipase. Thus, the fluorescence quenching of pancreatic lipase by NV-7 was a static quenching process [ 19 ], and the results are shown in Table S2 . With the increase of temperature, the number of binding sites between NV-7 and pancreatic lipase gradually decreased from 2 to 1, and Ka gradually decreased from 10.66 × 10 3 L/mol to 4.92 × 10 3 L/mol, indicating that there were two binding sites between NV-7 and pancreatic lipase, and the binding stability of one site to NV-7 was negatively correlated with temperature, which was converted from static quenching to dynamic quenching.…”

Hyperoside inhibits pancreatic lipase activity in vitro and reduces fat accumulation in vivo

“…The same result was also confirmed by the study of Ligupurpuroside B binding to lipase. 35 3.2 Effects of hyperoside on fat accumulation in high-fat diet-induced rats 3.2.1 Body weight, food intake, visceral weight and serum index. No obvious differences in the initial body weight and food intake were observed between these groups (Fig.…”