Interaction of rubratoxin B with serum albumin

Abstract

The interaction of rubratoxin B (RB) with bovine serum albumin (BSA) was investigated. Circular dichroism spectroscopy shows the interaction of RB with BSA as conformational change of BSA. Fluorescence quenching study suggests that RB binds to BSA at a few sites. At low concentration of RB, RB firstly binds to BSA at any binding sites far from Trp residues. By increasing RB concentration, RB binds to BSA at any binding sites near Trp residues.