Development of inhibitors against lipase and α-glucosidase from derivatives of monascus pigment

Abstract

New derivatives of monascus pigment were produced during Monascus fermentation by the addition of unnatural amino acids, and the inhibitory activities of the derivatives against diet-related lipase and alpha-glucosidase were tested. Derivatives with penicillamine (H-Pen), cyclohexylalanine (H-Cha), butylglycine (L-t-Bg), and norleucine (H-Nle) showed relatively high inhibitory activities against lipase. The H-Pen derivative exhibited the highest inhibitory activity, with an IC(50) (50% inhibition) value of 24.0 microM. The four derivatives all showed noncompetitive inhibition patterns against lipase. The inhibition constant (K(i)) of the H-Pen derivative was estimated to be 20.7 microM. The H-Pen derivative also exhibited a relatively high inhibitory activity against alpha-glucosidase, with an IC(50) value of 50.9 microM. The inhibition pattern of the H-Pen derivative against alpha-glucosidase appeared to be of a mixed type. The inhibition constants K(i) and were estimated to be 25.9, and 98.9 microM, respectively.

Synthesis and α-Glucosidase Inhibitory Mechanisms of Bis(2,3-dibromo-4,5-dihydroxybenzyl) Ether, a Potential Marine Bromophenol α-Glucosidase Inhibitor

“…This finding further supports the proposition that BDDE binds to the enzyme and slightly changes the secondary conformation of α-glucosidase. The increase in α-helix induced by BDDE is similar to α-glucosidase inhibitor penicillamine, which also induces an increase in the α-helix content [24]. However, BDDE-induced secondary structure changes are in contrast to other α-glucosidase inhibitors, for example, curcuminoids analogs [7], BIP [23], and hydroxycoumarin derivatives [25], all of which decrease the α-helix content in the enzyme molecule.…”

Inhibitory Activities ofCudrania tricuspidataLeaves on Pancreatic LipaseIn Vitroand LipolysisIn Vivo

“…The ability of the herbs to inhibit pancreatic lipase was measured using the method previously reported by Kim et al [9, 10]. Briefly, an enzyme buffer was prepared by the addition of 6  μ L porcine pancreatic lipase solution (Sigma-Aldrich) in buffer containing 10 mM MOPS (morpholinepropanesulphonic acid) and 1 mM EDTA, pH 6.8, to 169  μ L Tris buffer (100 mM Tris-HC1 and 5 mM CaCl 2 , pH 7.0).…”

A new pancreatic lipase inhibitor isolated from the roots of Actinidia arguta

“…The ability of the compounds to inhibit porcine pancreatic lipase was measured using the method previously reported by Kim et al (2007), with modifications. Briefly, an enzymebuffer was prepared by the addition of 30 PL (10 units) of a solution of porcine pancreatic lipase (Sigma, St. Louis, MO, U.S.A.) [in 10 mM MOPS (morpholinepropanesulphonic acid) and 1 mM EDTA, pH 6.8] to 850 PL of Tris buffer (100 mM Tris-HC1 and 5 mM CaCl 2 , pH 7.0).…”