Reexamining the diverse functions of arginine in biochemistry

Biochem Biophys Res Commun. 2024 Feb 27;705:149731. doi: 10.1016/j.bbrc.2024.149731. Online ahead of print.ABSTRACTArginine 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.PMID:38432110 | DOI:10.1016/j.bbrc.2024.149731

Source: Biochemical and Biophysical Research communications - March 3, 2024 Category: Biochemistry Authors: Munishwar Nath Gupta Vladimir N Uversky Source Type: research