Chaperone activity of antioxidant compounds to prevent the Aggregationof unfold proteins

Chaperone molecules play an important role in the proper folding of proteins and preventingproteinaggregation. Protein aggregation, a process which unnatural molecules connect together and createsoluble small oligomers or insoluble aggregations, depends on resistance conformation and colloidalcharacteristics of proteins. Finding proper ways to soften or gravel of proteins aggregation would beimportant in the control of diseases (e.g. Alzeimer s disease, Parkinsonism) that are related to thissituation.Seidlitziarosmarinus extract has antioxidant compounds which can cause increase in proteinsresistance and preventing from proteins aggregation. The aim of this study is to survey the effects ofantioxidant compounds in Seidlitziarosmarinus on proteins aggregation. In this research antioxidantproperties of Seidlitziarosmarinus extract was evaluated on ovotransferin, insulin, and alpha lacto albuminin the presence of DTT as an aggregation and settlement inducer factor, using visible light spectroscopy,indigenous florescence spectroscopy, ANS, and Near-UV spectroscopy. Results indicated that the extractof Seidlitziarosmarinus could prevent protein aggregation which was different between three subjects ofproteins and also there was a dose dependent manner about the extract; increase in concentration ofextract would promote the level of conservation.