Arginine and the Hofmeister Series: the role of ion-ion interactions in protein aggregation suppression.

ABSTRACT: L-Arginine hydrochloride is a very important aggregation suppressor for which there has been much attention given regarding elucidating its mechanism of action. Little consideration, however, has been given toward other salt forms besides chloride, even though the counterion likely imparts a large influence per the Hofmeister Series. Here, we report an in depth analysis of the role the counterion plays in the aggregation suppression behavior of arginine. Consistent with the empirical Hofmeister series, we found that the aggregation suppression ability of other arginine salt forms on a model protein (α-chymotrypsinogen) follows the order: H(2)PO(4)(-) > SO(4)(2-) > citrate(2-) > acetate(-) ≈ F(-) ≈ Cl(-) > Br(-) > I(-) ≈ SCN(-). Mechanistically, preferential interaction and osmotic virial c

SUBMITTER: Schneider CP 

PROVIDER: S-EPMC3110691 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature