A Conformationally Arrested Peptidomimetic Antibiotic Disrupts Selectively the Outer Membrane in Escherichia coli
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ABSTRACT: Using a shotgun proteomics approach, the expressed proteome of total membrane fractions of Escherichia coli ATCC25922 cells was analyzed under i) normal growth, and ii) treatment with the novel peptidomimetic JB-95 (a structurally arrested cyclic peptide). By selectively disrupturing the outer membrane (OM), this peptidomimetic displayed a novel mechanism of action and opens new avenues for developing antibiotics that specifically target the OM of Gram-negative bacteria.
INSTRUMENT(S):
ORGANISM(S): Escherichia Coli
SUBMITTER:
Christian Ahrens
LAB HEAD: Prof. John Robinson
PROVIDER: PXD002588 | Pride | 2015-12-07
REPOSITORIES: Pride
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