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Evaluation of chaperone ability of S. rosmarinus against protein aggregation
Abbas Heidari,Arezou Ghahghaei,Jafar Valizadeh 한국약제학회 2014 Journal of Pharmaceutical Investigation Vol.44 No.6
Protein aggregation occurs via a process inwhich unnatural molecules connect together and createsoluble small oligomers or insoluble aggregations. Theaggregation of protein depends on resistance conformationand the colloidal characteristics of proteins. Finding properways to stabilize or prevent of protein aggregation could beimportant for the control of such diseases as Alzheimer’sand Parkinson’s. Seidlitzia rosmarinus (S. rosmarinus)extract has antioxidant compounds which can cause anincrease in protein resistance and prevent protein aggregation. The aim of this study is to assess the chaperoneeffects of compounds in S. rosmarinus extract on proteinaggregation. In this research, the chaperone property of S. rosmarinus extract was evaluated on ovotransferin, insulin,and a-lactalbumin aggregation, using visible light spectroscopy,florescence and circular dichroism spectroscopy. The results indicate that the extract of S. rosmarinus couldprevent protein aggregation in a concentration-dependentmanner. The protective effect of S. rosmarinus, however,differed among the three proteins due to their differenthydrophobic surface areas.