Conformation of gramicidin A in phospholipid vesicles: circular dichroism studies of effects of ion binding, chemical modification, and lipid structure.
Conformation of gramicidin A in phospholipid vesicles: circular dichroism studies of effects of ion binding, chemical modification, and lipid structure.
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磷脂囊泡中短杆菌肽 A 的构象：离子结合、化学修饰和脂质结构影响的圆二色性研究。
DOI：
10.1021/bi00523a018
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发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Blout,ER
中科院分区：
文献类型：
--
作者：
Wallace,BA;Veatch,WR;Blout,ER
B。A. Wallace，* W. R. Veatch和E. R.摘要：用圆二色谱法研究了阳离子结合、化学修饰和脂质结构对短杆菌肽A在磷脂囊泡中的构象的影响，以帮助阐明这种抗生素的作用机制，并确定维持其膜结构所必需的特征。短杆菌肽A能够根据其所处环境的不同而采用多种不同的构象。在有机溶剂中，它形成双螺旋二聚体家族，而在膜中，它形成单螺旋的N-末端至N-末端二聚体。它在各种亲水性和两亲性有机溶剂中的结构都不能与其在膜中的结构等价。
B. A. Wallace,* W. R. Veatch, and E. R. Blout abstract: The effects of cation binding, chemical modifi-cation, and lipid structure on the conformation of the chan-nel-forming polypeptide gramicidin A in phospholipid vesicles have been investigated by circular dichroism spectroscopy in order to aid in elucidating the mechanism of action of this antibiotic and to ascertain features necessary for maintenance of its structure in membranes. Gramicidin A is capable of adopting a number of differentconformations, depending on its environment. In organic solvents, it forms a family of double-helical dimers, whereas in membranes, it forms an N-terminal to N-terminal dimer of single helices. None of the structures in a variety of hydrophilic and amphipathic organic solvents are equivalent to its structure in membranes.