Schwarz G, Blochmann U
Department of Biophysical Chemistry, Biocenter of the University, Basel, Switzerland.
FEBS Lett. 1993 Mar 1;318(2):172-6. doi: 10.1016/0014-5793(93)80015-m.
We have measured circular dichroism signals of aqueous mastoparan and mastoparan-X when titrated with electrically neutral phospholipid unilamellar vesicles. The data could be converted into association isotherms (binding curves) under various conditions of salt content. In spite of the absence of a net charge in the lipid moiety, substantial salt effects have been observed regarding the partition coefficient of the peptide and its conformation in the associated state. These results are discussed on the basis of a general thermodynamic approach for peptide association with lipid bilayers.
我们测量了用中性磷脂单层囊泡滴定的水溶性蜂毒素和蜂毒素-X的圆二色性信号。在不同盐含量条件下，这些数据可转化为缔合等温线（结合曲线）。尽管脂质部分没有净电荷，但在肽的分配系数及其缔合状态下的构象方面，已观察到显著的盐效应。基于肽与脂质双层缔合的一般热力学方法对这些结果进行了讨论。
