期刊
CHEMISTRY-A EUROPEAN JOURNAL
卷 20, 期 17, 页码 4948-4955出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201304562
关键词
conformational analysis; NOESY-NMR spectroscopy; peptide antibiotics; skyllamycin; structure elucidation
资金
- Cluster of Excellence (UniCat)
- German Research Council (DFG)
- Conseil Regional du Limousin
- Ministry of Education, Youth and Sports of the Czech Republic [CZ.1.05/2.1.00/03.0058]
Skyllamycin is a non-ribosomally synthesized cyclic depsipeptide from Streptomyces sp. Acta 2897 that inhibits PDGF-signaling. The peptide scaffold contains an N-terminal cinnamoyl moiety, a -methylation of aspartic acid, three -hydroxylated amino acids and one rarely occurring -hydroxy glycine. With the exception of -hydroxy glycine, the stereochemistry of the amino acids was assigned by comparison to synthetic reference amino acids applying chiral GC-MS and Marfey-HPLC analysis. The stereochemistry of -hydroxy glycine, which is unstable under basic and acidic conditions, was determined by conformational analysis, employing a combination of data from NOESY-NMR spectroscopy, simulated annealing and free MD simulations. The simulation procedures were applied for both R- and S-configured -hydroxy glycine of the skyllamycin structure and compared to the NOESY data. Both methods, simulated annealing and free MD simulations independently support S-configured -hydroxy glycine thus enabling the assignment of all stereocenters in the structure of skyllamycin and devising the role of two-component flavin dependent monooxygenase (Sky39) as S-selective.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据