Inhibition of protein aggregation: supramolecular assemblies of arginine hold the key.

ABSTRACT:

Background

Aggregation of unfolded proteins occurs mainly through the exposed hydrophobic surfaces. Any mechanism of inhibition of this aggregation should explain the prevention of these hydrophobic interactions. Though arginine is prevalently used as an aggregation suppressor, its mechanism of action is not clearly understood. We propose a mechanism based on the hydrophobic interactions of arginine.

Methodology

We have analyzed arginine solution for its hydrotropic effect by pyrene solubility and the presence of hydrophobic environment by 1-anilino-8-naphthalene sulfonic acid fluorescence. Mass spectroscopic analyses show that arginine forms molecular clusters in the gas phase and the cluster composition is dependent on the solution conditions. Light scattering studies indi

SUBMITTER: Das U 

PROVIDER: S-EPMC2064962 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature