Solution structure of termite-derived antimicrobial peptide, spinigerin, as determined in SDS micelle by NMR spectroscopy
Solution structure of termite-derived antimicrobial peptide, spinigerin, as determined in SDS micelle by NMR spectroscopy
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DOI：
10.1016/j.bbrc.2003.08.043
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发表时间：
2003-09-26
影响因子：
3.1
通讯作者：
Kim, Y
中科院分区：
文献类型：
--
作者：
Lee, KH;Shin, SY;Kim, Y
Spinigerin是一种来源于白蚁的线性抗菌肽。它由25个氨基酸组成，没有半胱氨酸。Spinigerin对革兰氏阳性菌和革兰氏阴性菌具有良好的溶解活性，但对人红细胞没有溶血活性。在这项研究中，我们提出了一个三维溶液结构的spinigerin在SDS胶束。根据CD数据，在TFE、DPC胶束和SDS胶束存在下，刺苷具有α-螺旋构象。通过NMR光谱测定的spinigerin的三维结构包含从Lys（4）到Thr（23）的稳定α-螺旋。Spinigerin（4-21）是一个从Lys（4）到Leu（21）的18个残基片段，与天然Spinigerin相比，含有类似含量的α-螺旋结构，并且发现也保留了抗菌活性。因此，这种α-螺旋结构和棘蛋白中的四个赖氨酸和三个精氨酸残基与膜表面上的磷脂的带负电荷的极性头部基团之间的强静电吸引在破坏膜和随后的细胞死亡中起重要作用。(C)2003年爱思唯尔公司All rights reserved.
Spinigerin is a linear antibacterial peptide derived from a termite insect. It consists of 25 amino acids and is devoid of cysteines. Spinigerin displays good lytic activities against Gram-positive and Gram-negative bacteria, but has no hemolytic activities against human erythrocytes. In this study, we present a three-dimensional solution structure of spinigerin in SDS micelles. According to CD data spinigerin has an alpha-helical conformation in the presence of TFE, DPC micelles, and SDS micelles. The three-dimensional structure of spinigerin as determined by NMR spectroscopy contains a stable alpha-helix from Lys(4) to Thr(23). Spinigerin (4-21), an 18-residue fragment from Lys(4) to Leu(21), contains a similar content of alpha-helical structure compared to native spinigerin and was found to retain antibacterial activity, too. Therefore, this alpha-helical structure and the strong electrostatic attraction between four Lys and three Arg residues in spinigerin and the negatively charged polar head groups of the phospholipids on the membrane surface play important roles in disrupting membrane and subsequent cell death. (C) 2003 Elsevier Inc. All rights reserved.