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• W2760002114 abstract "Abstract The reversibility and strength of the previously established dimerization of the important glycopeptide antibiotic vancomycin in four different aqueous solvents (including a medically-used formulation) have been studied using short-column sedimentation equilibrium in the analytical ultracentrifuge and model-independent SEDFIT-MSTAR analysis across a range of loading concentrations. The change in the weight average molar mass M w with loading concentration was consistent with a monomer-dimer equilibrium. Overlap of data sets of point weight average molar masses M w ( r ) versus local concentration c ( r ) for different loading concentrations demonstrated a completely reversible equilibrium process. At the clinical infusion concentration of 5 mg.mL −1 all glycopeptide is dimerized whilst at 19 µg.mL −1 (a clinical target trough serum concentration), vancomycin was mainly monomeric (<20% dimerized). Analysis of the variation of M w with loading concentration revealed dissociation constants in the range 25-75 μM, commensurate with a relatively weak association. The effect of two-fold vancomycin (19 µg.mL −1 ) appears to have no effect on the monomeric enterococcal VanS kinase involved in glycopeptide resistance regulation. Therefore, the 30% increase in sedimentation coefficient of VanS on adding vancomycin observed previously is more likely to be due to a ligand-induced conformational change of VanS to a more compact form rather than a ligand-induced dimerization." @default.
• W2760002114 created "2017-10-06" @default.
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• W2760002114 date "2017-10-05" @default.
• W2760002114 modified "2023-10-16" @default.
• W2760002114 title "Full hydrodynamic reversibility of the weak dimerization of vancomycin and elucidation of its interaction with VanS monomers at clinical concentration" @default.
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• W2760002114 doi "https://doi.org/10.1038/s41598-017-12620-z" @default.
• W2760002114 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5629194" @default.
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