In-cell DNP NMR reveals multiple targeting effect of antimicrobial peptide

IF 3.5 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Frances Separovic , Vinzenz Hofferek , Anthony P. Duff , Malcom J. McConville , Marc-Antoine Sani
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引用次数: 3

Abstract

Dynamic nuclear polarization NMR spectroscopy was used to investigate the effect of the antimicrobial peptide (AMP) maculatin 1.1 on E. coli cells. The enhanced 15N NMR signals from nucleic acids, proteins and lipids identified a number of unanticipated physiological responses to peptide stress, revealing that membrane-active AMPs can have a multi-target impact on E. coli cells. DNP-enhanced 15N-observed 31P-dephased REDOR NMR allowed monitoring how Mac1 induced DNA condensation and prevented intermolecular salt bridges between the main E. coli lipid phosphatidylethanolamine (PE) molecules. The latter was supported by similar results obtained using E. coli PE lipid systems. Overall, the ability to monitor the action of antimicrobial peptides in situ will provide greater insight into their mode of action.

Abstract Image

细胞内DNP核磁共振揭示抗菌肽的多靶向作用
采用动态核极化核磁共振波谱法研究抗菌肽(AMP)斑纹蛋白1.1对大肠杆菌细胞的影响。来自核酸、蛋白质和脂质的15N核磁共振信号增强,发现了许多意想不到的肽应激生理反应,揭示了膜活性amp可以对大肠杆菌细胞产生多靶点影响。dnp增强的15n -观察到31p去相的REDOR NMR可以监测Mac1如何诱导DNA缩聚并阻止主要大肠杆菌脂质磷脂酰乙醇胺(PE)分子之间的分子间盐桥。后者得到了大肠杆菌PE脂质系统类似结果的支持。总的来说,原位监测抗菌肽作用的能力将提供对其作用模式的更深入的了解。
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来源期刊
Journal of Structural Biology: X
Journal of Structural Biology: X Biochemistry, Genetics and Molecular Biology-Structural Biology
CiteScore
6.50
自引率
0.00%
发文量
20
审稿时长
62 days
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