Discovery of human pancreatic lipase inhibitors from root of Rhodiola crenulata via integrating bioactivity-guided fractionation, chemical profiling and biochemical assay

Inhibitory Potential of α-Amylase, α-Glucosidase, and Pancreatic Lipase by a Formulation of Five Plant Extracts: TOTUM-63

“…The family of compounds showing the strongest effect were the di-caffeoylquinic acids with 4.8, 6.2, 7.2, 9.4, and 11.4 times higher inhibitory activities on α-amylase than acarbose for cynarin, 1,5-dicaffeoylquinic acid, 3,4-dicaffeoylquinic acid, 3,5-dicaffeoylquinic acid, and 4,5-dicaffeoylquinic acid, respectively (based on IC 50 values) [ 51 ]. Similarly, significant lipase inhibitory activities have been shown for apigenin, oleanolic acid, anthocyanins, monocaffeoylquinic acids (including chlorogenic acid), dicaffeoylquinic acids (including cynarin), luteolin-7-O-glucoside, luteolin, and Eriodictyol [ 63 , 64 , 65 , 66 , 67 , 68 ]. The highest lipase inhibitions were obtained using luteolin-7-O-glucoside and eriodictyol, two flavonoids, with more than two times higher inhibitory activities than orlistat for both (based on IC 50 values) [ 68 ].…”

“…Similarly, significant lipase inhibitory activities have been shown for apigenin, oleanolic acid, anthocyanins, monocaffeoylquinic acids (including chlorogenic acid), dicaffeoylquinic acids (including cynarin), luteolin-7-O-glucoside, luteolin, and Eriodictyol [ 63 , 64 , 65 , 66 , 67 , 68 ]. The highest lipase inhibitions were obtained using luteolin-7-O-glucoside and eriodictyol, two flavonoids, with more than two times higher inhibitory activities than orlistat for both (based on IC 50 values) [ 68 ]. All these results confirm that α-amylase and lipase inhibitions by TOTUM-63 are not due to a single specific molecule, but that many molecules and families of molecules present in TOTUM-63 formulation contribute to these effects.…”

Potential hypoglycemic and hypolipidemic bioactive constituents in Cyclocarya paliurus leaves explored by affinity ultrafiltration with α‐glucosidase and pancreatic lipase

“…Peak 4 (kaempferol 3‐ O ‐rhamnoside) with the largest RBA value, presented the BE of −5.56 kcal/mol and theoretical IC 50 value of 84.23 μM, which were lower than those of the positive control orlistat. Kaempferol‐3‐ O ‐rhamnoside is flavonoid glycoside of kaempferol, which was also reported strong pancreatic lipase inhibition activity in a previous study (Ma et al, 2022). Meanwhile, kaempferol 3‐ O ‐rhamnoside could inhibit the lipase activity by shaping distinct interaction forces with amino acid residues ASN88, ASP249, ASP331, THR271, and TRP85 against H‐bonds, residue PHE335 against Pi‐Pi T‐shaped force, residue ALA332 against Pi‐Alkyl force, and residue LYS268 against Pi‐Cation and Pi‐Anion forces.…”

A rationally engineered specific near-infrared fluorogenic substrate of human pancreatic lipase for functional imaging and inhibitor screening

“…33,34 Although pPL and hPL have high amino acid sequence identity (86%) and a conserved catalytic triad (Asp-His-Ser), species differences in inhibitor responses towards these two lipases have been reported. 35 Consequently, the direct investigation of hPL and high-throughput screening of inhibitors have been realized as practical and reliable methods in complex biological systems.…”