Comprehensive overview of human serum albumin glycation in diabetes mellitus

Abstract

The presence of excess glucose in blood is regarded as a sweet hurt for patients with diabetes. Human serum albumin (HSA) is the most abundant protein in human plasma, which undergoes severe non-enzymatic glycation with glucose in patients with diabetes; this modifies the structure and function of HSA. Furthermore, the advanced glycation end products produced by glycated HSA can cause pathological damage to the human body through various signaling pathways, eventually leading to complications of diabetes. Many potential glycation sites on HSA have different degrees of sensitivity to glucose concentration. This review provides a comprehensive assessment of the in vivo glycation sites of HSA; it also discusses the effects of glycation on the structure and function of HSA. Moreover, it addresses the relationship between HSA glycation and diabetes complications. Finally, it focuses on the value of non-enzymatic glycation of HSA in diabetes-related clinical applications.

In vitro antioxidant, anti-glycation, and bile acid-lowering capacity of peanut milk fermented with Lactiplantibacillus plantarum Kinko-SU4

“…2 C. The concentration-dependent activity can be seen even in PM (36–65%) and increases significantly to 52–91% inhibition as a result of FPM. Albumin is abundant in serum and can be glycated at multiple sites, particularly in patients with diabetes mellitus ( Qiu et al, 2021 ). The effect of the extracts on all protein glycation stages was determined by the BSA-Fru model system ( Wang et al, 2011 ).…”

Discovery of novel glucosinolates inhibiting advanced glycation end products: Virtual screening and molecular dynamic simulation

“…SiteMap was utilized to assess and forecast the binding pocket for ligand attachment (Figure 2). Together with amino acids from previously published literature, the most efficient binding site was identified as follows 40,41 : Tyr 149, Arg 194, Arg198, Ser 191, Trp 213, Ser 214, Arg 217, Lys 221, Leu 237, His 241, Arg 256, Leu 259, Ala 290, Glu 291, and Lys 294 residues.…”

“…SiteMap was utilized to assess and forecast the binding pocket for ligand attachment (Figure 2). Together with amino acids from previously published literature, the most efficient binding site was identified as follows 40,41…”

Synthesis, Characterization, Antiglycation Evaluation, Molecular Docking, and ADMET Studies of 4-Thiazolidinone Derivatives

“…Subdomain I (A and B) is composed of residues 1–195, while II (A and B) spans from 196 to 383 and III (A and B) spans from 384 to 585. , It has been reported that the ligand (drug/compound) is mainly transported via binding through Sudlow sites II and III. Sudlow site I is located in subdomain IIA and Sudlow site II is located in subdomain IIIA . Molecular docking results also confirm this observation as compounds 1–4 interacted with different amino acids of the Sudlow sites II and III.…”