期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 20, 期 20, 页码 -出版社
MDPI
DOI: 10.3390/ijms20205152
关键词
antimicrobial peptide; microcin J25; epimerization; lasso peptide; mechanism of action
资金
- MINECO [CTQ2015-67870-P, CTQ2015-68677-R, EUIN2017-88320]
- Institute for Research in Biomedicine Barcelona (IRB Barcelona)
In this study, microcin J25, a potent antimicrobial lasso peptide that acts on Gram-negative bacteria, was subjected to a harsh treatment with a base in order to interrogate its stability and mechanism of action and explore its structure-activity relationship. Despite the high stability reported for this lasso peptide, the chemical treatment led to the detection of a new product. Structural studies revealed that this product retained the lasso topology, but showed no antimicrobial activity due to the epimerization of a key residue for the activity. Further microbiological assays also demonstrated that it showed a high synergistic effect with colistin.
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