LAUSR

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.