Structure-based analysis reveals hydration changes induced by arginine hydrochloride.
Arginine hydrochloride has been used to suppress protein aggregation during refolding and in various other applications. We investigated the structure of hen egg-white lysozyme (HEL) and solvent molecules in arginine hydrochloride solution by X-ray crystallography. Neither the backbone nor side-chain structure of HEL was altered by the presence of arginine hydrochloride. In addition, no stably bound arginine molecules were observed. The number of hydration water molecules, however, changed with the arginine hydrochloride concentration. We suggest that arginine hydrochloride suppresses protein aggregation by altering the hydration structure and the transient binding of arginine molecules that could not be observed.
Nakakido
Makoto
M
Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa 277-8562, Japan.
Tanaka
Yoshikazu
Y
Mitsuhori
Mariko
M
Kudou
Motonori
M
Ejima
Daisuke
D
Arakawa
Tsutomu
T
Tsumoto
Kouhei
K
D000818:Animals; D001120:Arginine / Q000737:chemistry*; D001622:Betaine / Q000737:chemistry; D002645:Chickens; D018360:Crystallography, X-Ray; D004527:Egg Proteins / Q000737:chemistry; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D012965:Sodium Chloride / Q000737:chemistry; D013395:Sucrose / Q000737:chemistry; D014867:Water / Q000737:chemistry
D004527:Egg Proteins; D014867:Water; D001622:Betaine; D012965:Sodium Chloride; D013395:Sucrose; D001120:Arginine; D009113:Muramidase