STRUCTURE AND ORIENTATION OF THE ANTIBIOTIC PEPTIDE MAGAININ IN MEMBRANES BY SOLID-STATE NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY
STRUCTURE AND ORIENTATION OF THE ANTIBIOTIC PEPTIDE MAGAININ IN MEMBRANES BY SOLID-STATE NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY
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DOI：
10.1002/pro.5560021208
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发表时间：
1993-12-01
期刊：
影响因子：
8
通讯作者：
OPELLA, SJ
中科院分区：
文献类型：
--
作者：
BECHINGER, B;ZASLOFF, M;OPELLA, SJ
爪蟾抗菌肽2是一种23个残基的肽，在膜环境中形成两亲性α-螺旋。它作为一种抗生素，已知会破坏许多细菌，真菌和一些肿瘤细胞细胞膜上的电化学梯度，尽管它不会溶解红细胞。一维和二维固态N-15 NMR光谱的具体N-15-标记爪蟾抗菌肽2定向双层样品表明，基本上整个肽的二级结构是α-螺旋，固定其与磷脂的相互作用，并定向平行于膜表面。
Magainin 2 is a 23-residue peptide that forms an amphipathic alpha-helix in membrane environments. It functions as an antibiotic and is known to disrupt the electrochemical gradients across the cell membranes of many bacteria, fungi, and some tumor cells, although it does not lyse red blood cells. One- and two-dimensional solid-state N-15 NMR spectra of specifically N-15-labeled magainin 2 in oriented bilayer samples show that the secondary structure of essentially the entire peptide is alpha-helix, immobilized by its interactions with the phospholipids, and oriented parallel to the membrane surface.