[The effect of phalloidin on stability of F- and G-actin]

Intrinsic tryptophan fluorescence and fluorescence of a hydrophobic probe bis-ANS were used to study the effect of phalloidin, a bicyclic heptapeptide toxin, on stability of monomeric (G) and polymeric (F) actin. It was found that bis-ANS fluorescence is sensitive to the actin polymerization process. Phalloidin in concentrations from 1 to 2 molecules per 1 actin molecule shifts the thermally induced unfolding transition in F-actin toward about 15 degrees C higher temperatures. The stabilizing effect of phalloidin is even more evident in the case of urea denaturation of F-actin. Moreover, phalloidin stabilizes against denaturing by not only F-actin, but G-actin as well, showing direct stabilizing interactions between phalloidin and G-actin.