Structure determination of lysobactin, a macrocyclic peptide lactone antibiotic
Structure determination of lysobactin, a macrocyclic peptide lactone antibiotic
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大环肽内酯抗生素溶杆菌素的结构测定
DOI：
10.1021/jo00266a029
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发表时间：
1989
影响因子：
3.6
通讯作者：
S. Unger
中科院分区：
文献类型：
--
作者：
A. Tymiak;T. J. McCormick;S. Unger
从溶杆菌发酵液中分离出一种新抗生素溶杆菌素 (1)。 ATCC 53042。溶菌素在体外被证明是对抗革兰氏阳性需氧和厌氧细菌的有效药物，其体内功效可与临床上有用的抗生素万古霉素相媲美。物理化学特性鉴定该抗生素为标称质量 1275 Da 的二元肽。溶杆菌素的结构，包括立体化学细节，是通过化学和酶降解的结合来确定的，这些降解主要通过质谱法进行分析。在合成修饰的基础上，溶杆菌素的大环内酯和N端D-氨基酸是有助于抗菌活性的重要结构元素。
A new antibiotic, lysobactin (1), was isolated from fermentations of Lysobacter sp. ATCC 53042. Lysobactin was shown to be a potent agent against Gram-positive aerobic and anaerobic bacteria invitro, and its efficacy in vivo was found to compare favorablywith the clinically useful antibiotic vancomycin. Physicochemical characterization identified the antibiotic as a dibasic peptide of nominal mass 1275 Da. The structure of lysobactin, including stereochemical details, was determined by a combination of chemical and enzymatic degradations that were analyzed primarily by mass spectrometry. On the basis of synthetic modifications, the macrocyclic lactone and N-terminal D-amino acid of lysobactin are important structural elements contributing to the antibacterial activity.