Structure-based analysis reveals hydration changes induced by arginine hydrochloride

Biophysical Chemistry
Makoto NakakidoKouhei Tsumoto

Abstract

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.

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Citations

Mar 3, 2015·Journal of Biomolecular Structure & Dynamics·Dhawal Shah, Abdul Rajjak Shaikh
Oct 10, 2009·Protein Expression and Purification·Ryosuke YumiokaDaisuke Ejima
Mar 5, 2016·Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan·Susumu Uchiyama
Jan 22, 2009·Biotechnology Journal·Tsutomu ArakawaA Hajime Koyama
Mar 2, 2011·Biotechnology Progress·Dhawal ShahRaj Rajagopalan
Jul 29, 2010·Protein Science : a Publication of the Protein Society·Alexander TischerChristian Lange
Sep 8, 2011·Biotechnology and Bioengineering·Melissa A HolsteinSteven M Cramer

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