Aggregation Suppression of Proteins by Arginine During Thermal Unfolding

Author(s): Tsutomu Arakawa, Yoshiko Kita, Daisuke Ejima, Kouhei Tsumoto, Harumi Fukada.

Journal Name: Protein & Peptide Letters

Volume 13 , Issue 9 , 2006

Become EABM
Become Reviewer


Arginine has been used to suppress aggregation of proteins during refolding and purification. We have further studied in this paper the aggregation-suppressive effects of arginine on two commercially important proteins, i.e., interleukine- 6 (IL-6) and a monoclonal antibody (mAb). These proteins show extensive aggregation in aqueous buffers when subjected to thermal unfolding. Arginine suppresses aggregation concentration-dependently during thermal unfolding. However, this effect was not specific to arginine, as guanidine hydrochloride (GdnHCl) at identical concentrations also was effective. While equally effective in aggregation suppression during thermal unfolding, arginine and GdnHCl differed in their effects on the structure of the native proteins. Arginine showed no apparent adverse effects on the native protein, while GdnHCl induced conformational changes at room temperature, i.e., below the melting temperature. These additives affected the melting temperature of IL-6 as well; arginine increased it concentration-dependently, while GdnHCl increased it at low concentration but decreased at higher concentration. These results clearly demonstrate that arginine suppresses aggregation via different mechanism from that conferred by GdnHCl.

Keywords: Arginine, aggregation suppression, interleulin-6, monoclonal antibody, protein stabilization

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2006
Page: [921 - 927]
Pages: 7
DOI: 10.2174/092986606778256171
Price: $58

Article Metrics

PDF: 10