Meyer H E, Heber M, Eisermann B, Korte H, Metzger J W, Jung G
Abteilung Biochemie Supramolekularer Systeme, Ruhr-Universität Bochum, Germany.
Anal Biochem. 1994 Dec;223(2):185-90. doi: 10.1006/abio.1994.1571.
Lantibiotics are antibiotic peptides produced via ribosomal synthesis of precursor proteins by gram-positive bacteria. They contain various unusual post-translational modifications, which include the formation of sulfide rings by lanthionine or beta-methyllanthionine, and 2,3-didehydroamino acids. The N-terminus may be blocked by a 2-oxobutyryl group and the C-terminus may be inaccessible in some of the lantibiotics. Due to these modifications the analysis of such peptides is very tedious. Chemical modifications using an ethanethiol-containing reaction mixture and/or trifluoroperacetic acid treatment were used to solve these analytical problems. Investigating the tetracyclic 22-peptide gallidermin and the N-terminally blocked tricyclic 34-peptide Pep5 as examples, a novel access to the primary structure of lantibiotics is demonstrated.
羊毛硫抗生素是革兰氏阳性菌通过核糖体合成前体蛋白产生的抗生素肽。它们含有各种不同寻常的翻译后修饰，包括由羊毛硫氨酸或β-甲基羊毛硫氨酸形成硫环，以及2,3-脱氢氨基酸。N端可能被2-氧代丁酰基封闭，在某些羊毛硫抗生素中C端可能无法接近。由于这些修饰，此类肽的分析非常繁琐。使用含乙硫醇的反应混合物进行化学修饰和/或三氟过乙酸处理来解决这些分析问题。以四环22肽加利德明和N端封闭的三环34肽Pep5为例进行研究，展示了一种确定羊毛硫抗生素一级结构的新方法。
