miglitol has been researched along with salacinol* in 3 studies
3 other study(ies) available for miglitol and salacinol
| Article | Year |
|---|---|
Elongation of the side chain by linear alkyl groups increases the potency of salacinol, a potent α-glucosidase inhibitor from the Ayurvedic traditional medicine "Salacia," against human intestinal maltase.
Four chain-extended analogs (12a-12d) and two related de-O-sulfonated analogs (13a and 13c) by introducing alkyl groups (a: R = C Topics: alpha-Glucosidases; Animals; Dose-Response Relationship, Drug; Glycoside Hydrolase Inhibitors; Humans; Intestines; Medicine, Ayurvedic; Molecular Conformation; Rats; Salacia; Structure-Activity Relationship; Sugar Alcohols; Sulfates | 2021 |
Hydrophobic substituents increase the potency of salacinol, a potent α-glucosidase inhibitor from Ayurvedic traditional medicine 'Salacia'.
Using an in silico method, seven analogs bearing hydrophobic substituents (8a: Me, 8b: Et, 8c: n-Pent, 8d: n-Hept, 8e: n-Tridec, 8f: isoBu and 8g: neoPent) at the 3'-O-position in salacinol (1), a highly potent natural α-glucosidase inhibitor from Ayurvedic traditional medicine 'Salacia', were designed and synthesized. In order to verify the computational SAR assessments, their α-glucosidase inhibitory activities were evaluated in vitro. All analogs (8a-8g) exhibited an equal or considerably higher level of inhibitory activity against rat small intestinal α-glucosidases compared with the original sulfonate (1), and were as potent as or higher in potency than the clinically used anti-diabetics, voglibose, acarbose or miglitol. Their activities against human maltase exhibited good relationships to the results obtained with enzymes of rat origin. Among the designed compounds, the one with a 3'-O-neopentyl moiety (8g) was most potent, with an approximately ten fold increase in activity against human maltase compared to 1. Topics: Animals; Glycoside Hydrolase Inhibitors; Humans; Hydrophobic and Hydrophilic Interactions; Intestine, Small; Medicine, Ayurvedic; Microsomes; Rats; Structure-Activity Relationship; Sugar Alcohols; Sulfates | 2016 |
Mapping the intestinal alpha-glucogenic enzyme specificities of starch digesting maltase-glucoamylase and sucrase-isomaltase.
Inhibition of intestinal α-glucosidases and pancreatic α-amylases is an approach to controlling blood glucose and serum insulin levels in individuals with Type II diabetes. The two human intestinal glucosidases are maltase-glucoamylase and sucrase-isomaltase. Each incorporates two family 31 glycoside hydrolases responsible for the final step of starch hydrolysis. Here we compare the inhibition profiles of the individual N- and C-terminal catalytic subunits of both glucosidases by clinical glucosidase inhibitors, acarbose and miglitol, and newly discovered glucosidase inhibitors from an Ayurvedic remedy used for the treatment of Type II diabetes. We show that features of the compounds introduce selectivity towards the subunits. Together with structural data, the results enhance the understanding of the role of each catalytic subunit in starch digestion, helping to guide the development of new compounds with subunit specific antidiabetic activity. The results may also have relevance to other metabolic diseases such as obesity and cardiovascular disease. Topics: 1-Deoxynojirimycin; Acarbose; alpha-Glucosidases; Catalytic Domain; Enzyme Inhibitors; Glycoside Hydrolase Inhibitors; Kinetics; Monosaccharides; Selenium Compounds; Starch; Sucrase-Isomaltase Complex; Sugar Alcohols; Sulfates | 2011 |