Suppression of Protein Aggregation by L-Arginine

Abstract

L-Arginine is one of the most commonly used and most generally applicable suppressors of protein aggregation. Its effect as enhancer of in vitro protein refolding was serendipitously discovered two decades ago. This article aims at giving a brief overview about the discovery of the arginine effect, the range of its applications that have been explored over the past two decades, and of the current state of the discussion regarding the mechanisms responsible for the action of L-arginine as suppressor of aggregation.

Arginine and proline applied as food additives stimulate high freeze tolerance in larvae of Drosophila melanogaster

“…Indeed, at relatively high concentrations, both proline and arginine were shown to directly interact with partially unfolded proteins, stabilizing them and preventing their further denaturation/ aggregation and/or assisting them in regaining their functional conformation. However, the theoretical mechanisms by which these stabilization effects are mediated are not yet fully understood and empirically confirmed (Lange and Rudolph, 2009;Schneider et al, 2011).…”

Tetramers Are the Activation-competent Species of the HOCl-specific Transcription Factor HypT

“…Arginine and NaCl are widely used as chemical additives to refold proteins and stabilize them against aggregation (17,19). Here, we used these additives as a tool to study HypT dissociation in a DNA-independent manner.…”

Preventing Aggregation of Recombinant Interferon beta-1b in Solution by Additives: Approach to an Albumin-Free Formulation

“…On the other hand, Shukla and Trout proposed the "gap effect" hypothesis. [28][29][30][31] Arginine may form a number of varying interactions with protein. Arginine increases surface tension and is larger than water (volume exclusion).…”