Reexamining the diverse functions of arginine in biochemistry

Abstract

Arginine in a free-state and as part of peptides and proteins shows distinct tendency to form clusters. In free-form, it has been found useful in cryoprotection, as a drug excipient for both solid and liquid formulations, as an aggregation suppressor, and an eluent in protein chromatography. In many cases, the mechanisms by which arginine acts in all these applications is either debatable or at least continues to attract interest. It is quite possible that arginine clusters may be involved in many such applications. Furthermore, it is possible that such clusters are likely to behave as intrinsically disordered polypeptides. These considerations may help in understanding the roles of arginine in diverse applications and may even lead to better strategies for using arginine in different situations.

Keywords: Arginine clusters; Chaperones; Cryoprotectants; Drug excipients; Intrinsically disordered proteins; Liquid-liquid phase separation; Osmolytes; Protein aggregation; Protein chromatography.