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Evaluation of chaperone ability of S. rosmarinus against protein aggregation

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Abstract

Protein aggregation occurs via a process in which unnatural molecules connect together and create soluble small oligomers or insoluble aggregations. The aggregation of protein depends on resistance conformation and the colloidal characteristics of proteins. Finding proper ways to stabilize or prevent of protein aggregation could be important for the control of such diseases as Alzheimer’s and Parkinson’s. Seidlitzia rosmarinus (S. rosmarinus) extract has antioxidant compounds which can cause an increase in protein resistance and prevent protein aggregation. The aim of this study is to assess the chaperone effects of compounds in S. rosmarinus extract on protein aggregation. In this research, the chaperone property of S. rosmarinus extract was evaluated on ovotransferin, insulin, and α-lactalbumin aggregation, using visible light spectroscopy, florescence and circular dichroism spectroscopy. The results indicate that the extract of S. rosmarinus could prevent protein aggregation in a concentration-dependent manner. The protective effect of S. rosmarinus, however, differed among the three proteins due to their different hydrophobic surface areas.

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Abbreviations

S. rosmarinus :

(Seidlitzia rosmarinus)

ANS:

1-Anilino-8-naphthalene sulfonic acid

DTT:

1,4-dithiothreitol

ThT:

(Thioflavin T)

CD:

(Circular dichroism)

Arg:

(Arginine)

Gly:

(Glycine)

Trp:

(tryptophan)

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Acknowledgments

This article dose not contain any studies with human and animal subjects performed by any of the authors. All authors (A. Heidari, A. Ghahghaei, and J. Valazadeh) declare that they have no conflict of interest. The authors are thankful to the university of Sistan and Baluchestan for providing necessary facilities.

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Correspondence to Arezou Ghahghaei.

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Heidari, A., Ghahghaei, A. & Valizadeh, J. Evaluation of chaperone ability of S. rosmarinus against protein aggregation. Journal of Pharmaceutical Investigation 44, 423–430 (2014). https://doi.org/10.1007/s40005-014-0136-1

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  • DOI: https://doi.org/10.1007/s40005-014-0136-1

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