Li Z Q, Merrifield R B, Boman I A, Boman H G
Rockefeller University, New York, NY 10021.
FEBS Lett. 1988 Apr 25;231(2):299-302. doi: 10.1016/0014-5793(88)80837-8.
Cecropin B and cecropin IA (sarcotoxin IA) are 35- and 39-residue antibacterial peptides from a silk moth and a meat fly, respectively. Using solid phase synthesis we have made these peptides as well as two 37-residue analogs, one containing a deletion of leucine and lysine (residues 2a and 2b) as compared to cecropin IA, the other containing an insertion of leucine and lysine at the corresponding place in cecropin B. This addition and removal of a lysine residue did not cause the expected change in electrophoretic mobility. When tested for antibacterial spectra, the insertion analog was found to be as active as the parent compound while the deletion analog had lost most of its antibacterial capacity. In addition it was shown that the C-terminal amide contributes to the broad spectrum properties of the cecropins.
天蚕素B和天蚕素IA（肌毒素IA）分别是来自蚕蛾和肉蝇的由35个和39个氨基酸残基组成的抗菌肽。我们采用固相合成法制备了这些肽以及两种由37个氨基酸残基组成的类似物，一种与天蚕素IA相比缺失了亮氨酸和赖氨酸（第2a和2b位残基），另一种在天蚕素B的相应位置插入了亮氨酸和赖氨酸。赖氨酸残基的这种添加和去除并未引起预期的电泳迁移率变化。在测试抗菌谱时，发现插入类似物与母体化合物具有相同的活性，而缺失类似物则大部分丧失了其抗菌能力。此外，还表明C末端酰胺有助于天蚕素的广谱特性。
