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Gastric stability and oral bioavailability of colistin sulfate in pigs challenged or not with Escherichia coli O149: F4 (K88)

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Academic year: 2021

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Figure

Fig. 1.  The colistin structure is composed of a hydrophilic cycloheptapeptide ring with three positively charged amine groups, a tail tripeptide moiety with two positively charged amine groups, and a hydrophobic acyl chain tail.
Fig. 2. Degradation profile of colistin sulfate (CS): Evolution of CS concentrations over time in a simulated gastric fluid (SGF) as obtained by HPLC-MS/MS
Fig. 3.  Degradation products  (M1, M2, M3, and M4)  of  colistin sulfate (CS)  formed by the enzymatic action of pepsin on peptide bonds in the CS side chain
Fig.   4.  Mean   log   2   of   dilution   factor  ±   standard   deviation   (SD)   of  minimum   inhibitory concentration (MIC) value distributions of non-degraded (t=0) and degraded colistin sulfate (CS) against  E
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