Vedenkina N S, Kalinichenko L P, Permiakov E A
Mol Biol (Mosk). 1995 May-Jun;29(3):597-602.
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.
利用内源性色氨酸荧光和疏水性探针双-ANS的荧光来研究双环七肽毒素鬼笔环肽对单体肌动蛋白（G）和聚合肌动蛋白（F）稳定性的影响。发现双-ANS荧光对肌动蛋白聚合过程敏感。每1个肌动蛋白分子中含1至2个分子的鬼笔环肽会使F-肌动蛋白的热诱导解折叠转变温度升高约15摄氏度。在F-肌动蛋白的尿素变性实验中，鬼笔环肽的稳定作用更为明显。此外，鬼笔环肽不仅能稳定F-肌动蛋白，也能稳定G-肌动蛋白，表明鬼笔环肽与G-肌动蛋白之间存在直接的稳定相互作用。
