TY - JOUR
T1 - Structure-based analysis reveals hydration changes induced by arginine hydrochloride
AU - Nakakido, Makoto
AU - Tanaka, Yoshikazu
AU - Mitsuhori, Mariko
AU - Kudou, Motonori
AU - Ejima, Daisuke
AU - Arakawa, Tsutomu
AU - Tsumoto, Kouhei
N1 - Funding Information:
This work was supported in part by the National Project on Protein Structural and Functional Analyses (Ministry of Education, Culture, Sports, Science, and Technology of Japan). It was also supported in part by Grants-in-Aid for General Research (K.T.) and Younger Scientists (Y.T.) from the Ministry of Education, Science, Sports, and Culture of Japan.
PY - 2008/10
Y1 - 2008/10
N2 - 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.
AB - 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.
KW - Arginine hydrochloride
KW - Crystal structure
KW - Hydration water molecules
KW - Lysozyme
KW - Protein aggregation
KW - Refolding
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U2 - 10.1016/j.bpc.2008.07.009
DO - 10.1016/j.bpc.2008.07.009
M3 - Article
C2 - 18725174
AN - SCOPUS:51649101489
VL - 137
SP - 105
EP - 109
JO - Biophysical Chemistry
JF - Biophysical Chemistry
SN - 0301-4622
IS - 2-3
ER -