Tamamura H, Kuroda M, Masuda M, Otaka A, Funakoshi S, Nakashima H, Yamamoto N, Waki M, Matsumoto A, Lancelin J M
Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
Biochim Biophys Acta. 1993 May 13;1163(2):209-16. doi: 10.1016/0167-4838(93)90183-r.
The solution structure of tachyplesin I, which was isolated from membrane acid extracts of the hemocytes from the Japanese horseshoe crab (Tachypleus tridentatus), was determined by nuclear magnetic resonance (NMR) and distance geometry calculation. Tachyplesin I takes an antiparallel beta-sheet structure with a type-II beta-turn. Recently, among more than 20 synthetic peptides associated with tachyplesin and its isopeptide (polyphemusin), we found that a novel compound, which we designated as T22 ([Tyr5,12, Lys7]-polyphemusin II), strongly inhibited the human immunodeficiency virus (HIV)-1-induced cytopathic effect and viral antigen expression. The solution structure of T22 was investigated using NMR, and its secondary structure was confirmed to be similar to that of tachyplesin I. The anti-parallel beta-sheet structure and the several amino-acid side chains on the plane of the beta-sheet of T22 are thought to be associated with the expression of anti-HIV activity.
从日本鲎（三刺鲎）血细胞的膜酸提取物中分离得到的鲎素I的溶液结构，通过核磁共振（NMR）和距离几何计算得以确定。鲎素I呈具有II型β-转角的反平行β-折叠结构。最近，在20多种与鲎素及其异肽（鲎抗菌肽）相关的合成肽中，我们发现了一种新型化合物，我们将其命名为T22（[酪氨酸⁵,¹², 赖氨酸⁷]-鲎抗菌肽II），它能强烈抑制人类免疫缺陷病毒（HIV）-1诱导的细胞病变效应和病毒抗原表达。利用核磁共振对T22的溶液结构进行了研究，其二级结构被证实与鲎素I相似。T22的反平行β-折叠结构以及β-折叠平面上的几个氨基酸侧链被认为与抗HIV活性的表达有关。
