Naghmeh Sattarahmady, Ali A. Moosavi-Movahedi,
Volume 7, Issue 1 (7-2007)
Abstract
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.
Raziyeh Gharib, Ali Khatibi,
Volume 21, Issue 5 (1-2022)
Abstract
Background: Glycation is the non-enzymatic reaction between the carbonyl groups in sugar and free amino groups in proteins. this reaction leads to changes in structure and functions of proteins. Advanced glycation end products (AGEs) is the final stage in this process, which is highly oxidizing and destructive nature, causing many diabetic complications.
Methods: In the present investigation, the effect of fasting upon the glycation process of human Carbonic anhydrase II under physiological conditions (37 °C and pH 7.4) was studied recruiting various techniques including Ultraviolet–visible spectroscopy, fluorescence spectroscopy and CD Spectroscopy. To address this question, different samples of control carbonic anhydrase (without glucose and 3-beta-hydroxybutyrate), carbonic anhydrase with glucose, carbonic anhydrase in the presence of only 3-beta-hydroxybutyrate (BHB) and carbonic anhydrase along with glucose and 3-beta-hydroxybutyrate were incubated for 35 days under physiological conditions.
Results: The results indicate that 3-beta-hydroxybutyrate, which is greatly increased in the body during fasting, functions as an inhibitor of the glycation process and decreases the impacts of glucose binding to the protein and prevents the formation of AGEs and preserve enzyme activity.
Conclusion: Fasting can play an important role in maintaining the health of the body and eliminating the complications of the disease, with a significant increase in the production of 3-beta-hydroxybutyrate as an inhibitor of the glycation process.
