MINIREVIEW ON STRUCTURAL CHANGES OF GLYCATED HUMAN SERUM ALBUMIN

The interaction of reducing carbohydrates with proteins leads to a cascade of reactions that are known as glycation or Maillard reaction that have important roles in diabetic complications. In this minireview, structural changes of glycated human serum albumin (GHSA) via various sugars in different incubation times, which reported in scientific literature as well as our research, were reported. Our studies showed glycation induced structural changes for Human Serum Albumin (HSA). In glycation process of HSA after 21 days incubation, glucose separates from HSA and induced the formation of molten globule state that is relative to several diseases that originate from molten globule state in proteins. Also, glycation of HSA induced aggregation states and amyloid formation as well as decreased surface tension which plays a role of denaturant for protein as a surfactant. In following, we showed that alginate as a sugar polymer decreased glycation reaction in HSA. Finally, it is compared the structural changes of artificial and in vitro interaction of sugars with HSA as well as diabetic patients HSA. The results show the number of arginine residues in HSA of diabetic patients is more modified relative to lab samples.