蜂毒肽的一种合成类似物会聚集成大的寡聚体。
A synthetic analogue of melittin aggregates in large oligomers.
作者信息
John E, Jähnig F
机构信息
Max-Planck-Institut für Biologie, Tübingen, Germany.
出版信息
Biophys J. 1992 Dec;63(6):1536-43. doi: 10.1016/S0006-3495(92)81737-X.
Abstract
An analogue of melittin synthesized in the group of E. T. Kaiser (DeGrado, W. F., F. J. Keźdy, and E. T. Kaiser. 1981. J. Am. Chem. Soc. 103:679-681) was investigated by Raman spectroscopy and fluorescence anisotropy decay. In water, the analogue is completely alpha-helical and aggregates in large oligomers of about 50 monomers. In vesicle membranes, it undergoes orientational fluctuations similar to melittin. The most significant difference from melittin, therefore, is the formation of straight helixes and their aggregation in large oligomers in water. We interpret this as a consequence of the lacking proline residue in the analogue. We, furthermore, hypothesize that the increased tendency for aggregation causes the increased hemolytic activity of the analogue.
摘要
E. T. 凯泽团队合成的一种蜂毒肽类似物（德格拉多，W. F.，F. J. 凯兹迪，和E. T. 凯泽。1981年。《美国化学会志》103:679 - 681）通过拉曼光谱和荧光各向异性衰减进行了研究。在水中，该类似物完全呈α螺旋结构，并聚集形成约50个单体的大寡聚体。在囊泡膜中，它经历类似于蜂毒肽的取向波动。因此，与蜂毒肽最显著的差异在于在水中形成直螺旋及其在大寡聚体中的聚集。我们将此解释为该类似物中缺乏脯氨酸残基的结果。此外，我们推测聚集倾向的增加导致了该类似物溶血活性的增加。
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