Determination of binding constants between the antibiotic ristocetin A and D-Ala-D-Ala terminus peptides by affinity capillary electrophoresis |
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Authors: | M Azad L Hernandez A Plazas M Rudolph F A Gomez |
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Institution: | (1) Department of Chemistry and Biochemistry, California State University, 5151 State University Drive, 90032-8202 Los Angeles, CA, USA |
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Abstract: | Summary Binding constants between the antibiotic ristocetin A (Rist A) and D-Ala-D-Ala terminus peptides were determined using affinity
capillary electrophoresis (ACE). In these experiments two techniques are used to obtain binding constants. In the first, a
plug of Rist A and non-interacting standards are injected and electrophoresed. Analysis of the change in the relative migration
time ratio (RMTR) of Rist, relative to the non-interacting standards, as a function of the concentration of peptide, yields a value for the
binding constant (Kb). In the second, samples of peptide and standards are injected and electrophoresed in increasing concentrations of Rist A
in the running buffer. Analysis using theRMTR yields aK
b. The findings described here demonstrate the advantage of using ACE for estimating binding parameters between antibiotics
and ligands. |
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Keywords: | Affinity capillary electrophoresis Antibiotics Binding constants Ristocetin |
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