title: Review: Why is arginine effective in suppressing aggregation?
abstract: Arginine is finding a wide range of applications in production of proteins. Arginine has been used for many years to assist protein refolding. This effect was ascribed to aggregation suppression by arginine of folding intermediates during protein refolding. Recently, we have observed that arginine facilitates elution of antibodies during Protein-A chromatography and solubilizes insoluble proteins from inclusion bodies, which both can be ascribed to weakening of protein-protein interactions. In order to gain understanding on why arginine is effective in reducing protein-protein interactions and suppressing aggregation, the effects of arginine on stability and solubility of pure proteins have been examined, which showed that arginine is not a protein-stabilizer, but is an aggregation suppressor. However, there is no explanation proposed so far on why arginine suppresses aggregation of proteins. This review addresses such question and then attempts to show differences between arginine and strong denaturants, which are also known as an aggregation suppressor.
authors.affiliation: Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Sendai, Japan.
authors.forename: Kohei
authors.initials: K
authors.lastname: Tsumoto
authors.forename: Daisuke
authors.initials: D
authors.lastname: Ejima
authors.forename: Yoshiko
authors.initials: Y
authors.lastname: Kita
authors.forename: Tsutomu
authors.initials: T
authors.lastname: Arakawa
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D001120:Arginine / Q000737:chemistry / Q000494:pharmacology*; D011489:Protein Denaturation / Q000187:drug effects; D017510:Protein Folding; D012995:Solubility / Q000187:drug effects; D013500:Surface Tension / Q000187:drug effects
chemical_list: D000596:Amino Acids; D001120:Arginine