Comparative study of thermal domains analyzing of glycated and nonglycated human serum albumin

Resistance of a protein against a denaturant agent is a useful property. Protein biological functiondependson its native structure. The loss of this folded structure leads to inactivate of a protein.[1,2]. Proteinunfolding can be reversible or irreversible. The unfolding reversibility of manyproteins has been studiedusing different denaturant agents such as chemical reagents andtemperature [3]. Irreversibility causesmisfolding and aggregation of proteins in cells and underin vitro conditions. Most importantly, it isinvolved in a wide range of diseases, including someof the most prevalent neurodegenerative disorders[4]. In the current research, the domainsthermal unfolding of glycated human serum albumin (GHSA) andhuman serum albumin (HSA)were studied under incubation at physiological conditions for 35 days. The domains thermalunfolding ofGHSA and HSA were evaluated using differential scanning calorimetry (DSC),circular dichroism (CD),and UV–Vis spectroscopy. The results showed that the first energeticdomain of GHSA remained aftercooling back from 80 ºC,while the first energetic domain ofHSA disappeared at thistemperature.Moreover, the secondenergetic domain of GHSA kepton after cooling back from 90 ºC, but itdisappeared in HSA atthis temperate. Also, the secondarystructure recovery after cooling back in GHSAwas higherthan HSA. Therefore, according to the obtained results,glucose can act as a stabilizer forHSAdomains and can be used in food and pharmaceutical industries.

کلیدواژه ها:

Glycation ، Domain ، Human serum albumin ، Thermal resistans protein ، DSC