Determination of the secondary structure of selected melittin analogues with different haemolytic activities.
Determination of the secondary structure of selected melittin analogues with different haemolytic activities.
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DOI：
10.1042/bj2990587
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发表时间：
1994-04
期刊：
影响因子：
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通讯作者：
E. Pérez-Payá;R. Houghten;S. Blondelle
中科院分区：
文献类型：
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作者：
E. Pérez-Payá;R. Houghten;S. Blondelle
在早期的研究中，我们已经报道了蜂毒蛋白氨基酸序列的微小改变会导致其生物活性的巨大变化。在目前的研究中，我们研究了溶血活性增加或降低的蜂毒素类似物的二级结构，以进一步了解溶液中肽结合和/或插入磷脂膜的结构特征。这是通过分析不同离子强度溶液中类似物的cd光谱来完成的，并且在胶束存在的情况下。这些研究允许评估小序列修饰（即单个氨基酸的遗漏或取代）对水溶液中蜂毒素自结合诱导的二级结构的影响，以及其与胶束的结合亲和力。结果表明，两亲性、链间距离和疏水残基的取向都参与了稳定结构的诱导。
In earlier studies, we have reported that minor modifications in the amino acid sequence of melittin result in dramatic changes in its biological activity. In the current study, we have investigated the secondary structure of melittin analogues with either increased or decreased haemolytic activity in order to further our understanding of the structural features involved in the binding and/or insertion of peptides into a phospholipid membrane from solution. This was accomplished by analysing the c.d. spectra of the analogues in solutions of various ionic strength and, separately, in the presence of micelles. These studies permit the assessment of the effect of small sequence modifications (i.e. single amino acid omission or substitution) on the self-association-induced secondary structure of melittin in aqueous solution, as well as its binding affinity to micelles. It was found that amphipathicity, as well as interchain distances and the orientation of hydrophobic residues, were involved in the induction of stabilized structures.