Structure and Antidiabetic Activity of a Glycoprotein from Porphyra haitanensis

• DOI: 10.1021/acs.jafc.3c04276
• Publication Date: 2023-10-25T09:52:32Z
• Authors: Yujia Ou; Lijingting Xu; Mingrong Chen; Xiaodan Lu; Zebin Guo; Baodong Zheng
• Keywords: Hydrophobic effect; Glycosidic bond; Tetramer

A novel antidiabetic glycoprotein (PG) was isolated and purified from Porphyra haitanensis, its structure inhibiting activity on α-amylase α-glucosidase were analyzed. The purity of the PG 95.29 ± 0.21%, molecular weight 163.024 5.55 kDa. had a tetramer with α- β-subunits, it contained 54.12 0.86% protein (with highly hydrophobic amino acids) 41.19% 0.64% carbohydrate (composed galactose). linked via an O-glycosidic bond, exhibiting α-helical high stability. In addition, inhibited activities α-glucosidase, by changing enzyme's toward PG's in noncompetitive inhibition mode. Molecular docking results showed that interaction, whereas hydrogen bonds interaction. Overall, to polysaccharides bonds, showing configuration effect, which altered exerted hypoglycemic activity. This study provides insights into analyzing glycoproteins.