Hypoglycemic Efficacy of Docking Selected Natural Compounds against α-Glucosidase and α-Amylase. 2018

Jirawat Riyaphan, and Chien-Hung Jhong, and Shian-Ren Lin, and Chia-Hsiang Chang, and May-Jwan Tsai, and Der-Nan Lee, and Ping-Jyun Sung, and Max K Leong, and Ching-Feng Weng
Department of Life Science and Institute of Biotechnology, National Dong-Hwa University, Hualien 97401, Taiwan. mecurry@gmail.com.

The inhibition of α-glucosidase and α-amylase is a clinical strategy for the treatment of type II diabetes, and herbal medicines have been reported to credibly alleviate hyperglycemia. Our previous study has reported some constituents from plant or herbal sources targeted to α-glucosidase and α-amylase via molecular docking and enzymatic measurement, but the hypoglycemic potencies in cell system and mice have not been validated yet. This study was aimed to elucidate the hypoglycemic efficacy of docking selected compounds in cell assay and oral glucose and starch tolerance tests of mice. All test compounds showed the inhibition of α-glucosidase activity in Caco-2 cells. The decrease of blood sugar levels of test compounds in 30 min and 60 min of mice after OGTT and OSTT, respectively and the decreased glucose levels of test compounds were significantly varied in acarbose. Taken altogether, in vitro and in vivo experiments suggest that selected natural compounds (curcumin, antroquinonol, HCD, docosanol, tetracosanol, rutin, and actinodaphnine) via molecular docking were confirmed as potential candidates of α-glucosidase and α-amylase inhibitors for treating diabetes.

UI MeSH Term Description Entries
D007004 Hypoglycemic Agents Substances which lower blood glucose levels. Antidiabetic,Antidiabetic Agent,Antidiabetic Drug,Antidiabetics,Antihyperglycemic,Antihyperglycemic Agent,Hypoglycemic,Hypoglycemic Agent,Hypoglycemic Drug,Antidiabetic Agents,Antidiabetic Drugs,Antihyperglycemic Agents,Antihyperglycemics,Hypoglycemic Drugs,Hypoglycemic Effect,Hypoglycemic Effects,Hypoglycemics,Agent, Antidiabetic,Agent, Antihyperglycemic,Agent, Hypoglycemic,Agents, Antidiabetic,Agents, Antihyperglycemic,Agents, Hypoglycemic,Drug, Antidiabetic,Drug, Hypoglycemic,Drugs, Antidiabetic,Drugs, Hypoglycemic,Effect, Hypoglycemic,Effects, Hypoglycemic
D001786 Blood Glucose Glucose in blood. Blood Sugar,Glucose, Blood,Sugar, Blood
D004791 Enzyme Inhibitors Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction. Enzyme Inhibitor,Inhibitor, Enzyme,Inhibitors, Enzyme
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000516 alpha-Amylases Enzymes that catalyze the endohydrolysis of 1,4-alpha-glycosidic linkages in STARCH; GLYCOGEN; and related POLYSACCHARIDES and OLIGOSACCHARIDES containing 3 or more 1,4-alpha-linked D-glucose units. Taka-Amylase A,alpha-Amylase,Alpha-Amylase Bayer,Maxilase,Mégamylase,alpha-1,4-D-Glucanglucanohydrolase,Alpha Amylase Bayer,AlphaAmylase Bayer,Taka Amylase A,TakaAmylase A,alpha 1,4 D Glucanglucanohydrolase,alpha Amylase,alpha Amylases
D000520 alpha-Glucosidases Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-glucose. Deficiency of alpha-1,4-glucosidase may cause GLYCOGEN STORAGE DISEASE TYPE II. Acid Maltase,Lysosomal alpha-Glucosidase,Maltase,Maltases,Maltase-Glucoamylase,Neutral Maltase,Neutral alpha-Glucosidase,alpha-Glucosidase,Lysosomal alpha Glucosidase,Maltase Glucoamylase,Neutral alpha Glucosidase,alpha Glucosidase,alpha Glucosidases,alpha-Glucosidase, Lysosomal,alpha-Glucosidase, Neutral
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001688 Biological Products Complex pharmaceutical substances, preparations, or matter derived from organisms usually obtained by biological methods or assay. Biologic,Biologic Drug,Biologic Product,Biological,Biological Drug,Biological Medicine,Biological Product,Biologics,Biopharmaceutical,Natural Product,Natural Products,Biologic Drugs,Biologic Medicines,Biologic Pharmaceuticals,Biologic Products,Biological Drugs,Biological Medicines,Biologicals,Biopharmaceuticals,Products, Biological,Drug, Biologic,Drug, Biological,Drugs, Biologic,Drugs, Biological,Medicine, Biological,Medicines, Biologic,Medicines, Biological,Pharmaceuticals, Biologic,Product, Biologic,Product, Biological,Product, Natural
D051379 Mice The common name for the genus Mus. Mice, House,Mus,Mus musculus,Mice, Laboratory,Mouse,Mouse, House,Mouse, Laboratory,Mouse, Swiss,Mus domesticus,Mus musculus domesticus,Swiss Mice,House Mice,House Mouse,Laboratory Mice,Laboratory Mouse,Mice, Swiss,Swiss Mouse,domesticus, Mus musculus
D056004 Molecular Dynamics Simulation A computer simulation developed to study the motion of molecules over a period of time. Molecular Dynamics Simulations,Molecular Dynamics,Dynamic, Molecular,Dynamics Simulation, Molecular,Dynamics Simulations, Molecular,Dynamics, Molecular,Molecular Dynamic,Simulation, Molecular Dynamics,Simulations, Molecular Dynamics

Related Publications

Jirawat Riyaphan, and Chien-Hung Jhong, and Shian-Ren Lin, and Chia-Hsiang Chang, and May-Jwan Tsai, and Der-Nan Lee, and Ping-Jyun Sung, and Max K Leong, and Ching-Feng Weng
January 2017, Current topics in medicinal chemistry,
Jirawat Riyaphan, and Chien-Hung Jhong, and Shian-Ren Lin, and Chia-Hsiang Chang, and May-Jwan Tsai, and Der-Nan Lee, and Ping-Jyun Sung, and Max K Leong, and Ching-Feng Weng
July 2021, Journal of bioscience and bioengineering,
Jirawat Riyaphan, and Chien-Hung Jhong, and Shian-Ren Lin, and Chia-Hsiang Chang, and May-Jwan Tsai, and Der-Nan Lee, and Ping-Jyun Sung, and Max K Leong, and Ching-Feng Weng
October 2022, Life (Basel, Switzerland),
Jirawat Riyaphan, and Chien-Hung Jhong, and Shian-Ren Lin, and Chia-Hsiang Chang, and May-Jwan Tsai, and Der-Nan Lee, and Ping-Jyun Sung, and Max K Leong, and Ching-Feng Weng
January 2020, Bioorganic chemistry,
Jirawat Riyaphan, and Chien-Hung Jhong, and Shian-Ren Lin, and Chia-Hsiang Chang, and May-Jwan Tsai, and Der-Nan Lee, and Ping-Jyun Sung, and Max K Leong, and Ching-Feng Weng
January 2022, Journal of biomolecular structure & dynamics,
Jirawat Riyaphan, and Chien-Hung Jhong, and Shian-Ren Lin, and Chia-Hsiang Chang, and May-Jwan Tsai, and Der-Nan Lee, and Ping-Jyun Sung, and Max K Leong, and Ching-Feng Weng
July 2020, Food chemistry,
Jirawat Riyaphan, and Chien-Hung Jhong, and Shian-Ren Lin, and Chia-Hsiang Chang, and May-Jwan Tsai, and Der-Nan Lee, and Ping-Jyun Sung, and Max K Leong, and Ching-Feng Weng
June 2019, Molecules (Basel, Switzerland),
Jirawat Riyaphan, and Chien-Hung Jhong, and Shian-Ren Lin, and Chia-Hsiang Chang, and May-Jwan Tsai, and Der-Nan Lee, and Ping-Jyun Sung, and Max K Leong, and Ching-Feng Weng
March 2011, International journal of food sciences and nutrition,
Jirawat Riyaphan, and Chien-Hung Jhong, and Shian-Ren Lin, and Chia-Hsiang Chang, and May-Jwan Tsai, and Der-Nan Lee, and Ping-Jyun Sung, and Max K Leong, and Ching-Feng Weng
March 2023, Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy,
Jirawat Riyaphan, and Chien-Hung Jhong, and Shian-Ren Lin, and Chia-Hsiang Chang, and May-Jwan Tsai, and Der-Nan Lee, and Ping-Jyun Sung, and Max K Leong, and Ching-Feng Weng
August 2023, Journal of the science of food and agriculture,
Copied contents to your clipboard!