多糖
化学
生物化学
硫酸化
二肽基肽酶
IC50型
酶
体外
作者
Anjaly Thambi,Kajal Chakraborty
标识
DOI:10.1080/14786419.2022.2140660
摘要
Dipeptidyl peptidase is a crucial enzyme that regulates glucose metabolism by degrading incretins, such as glucagon-like-peptide-1, thereby reducing insulin secretion from the pancreatic β-cells. Consequently, dipeptidyl peptidase-IV inhibitors are an important remedial approach to moderate the hyperglycemic pathophysiology. A pyruvylated polysaccharide characterized as [→3)-4,6-O-(1-carboxyethylidene)-β-D-galp-(2SO3-)-(1→4)-3,6-α-L-AnGalp-(2OMe)-(1→], isolated from the marine macroalga Hydropuntia edulis, showed attenuation potential against dipeptidyl peptidase-IV (IC50 4.44 μM). The structure was elucidated using mass and one/two-dimensional nuclear magnetic resonance spectroscopic analyses of hydrolyzed polysaccharide besides glycosidic linkages obtained from partially methylated alditol acetate derivative. The isolated polysaccharide also revealed potential anti-carbolytic properties against α-amylase/α-glucosidase (IC50 45-47 μM). The results proved the candidacy of pyruvylated polysaccharide isolated from H. edulis as a potential therapeutic lead against hyperglycemia.
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