Current Pharmaceutical Biotechnology

Zeno Foldes-Papp
Visiting Professor of Medical Biochemistry
HELIOS Clinical Center of Emergency Medicine
Department for Internal Medicine
Alte-Koelner-Strasse 9
D-51688 Koeln-Wipperfuerth


Suppression of Protein Aggregation by L-Arginine

Author(s): Christian Lange and Rainer Rudolph

Affiliation: Institute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes- Str. 3, 06120 Halle (Saale), Germany.


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.

Keywords: Arginine, in vitro-refolding, protein aggregation, aggregation suppressor

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Article Details

Page: [408 - 414]
Pages: 7
DOI: 10.2174/138920109788488851
Price: $58