Use of affinity capillary electrophoresis to determine binding constants of polyethylene glycol (PEG)-vancomycin and linked teicoplanin species to peptide ligands

ANYL 147

Lilia Hernandez, aupbfe@yahoo.com, Chemistry, California State University, 1515 University Dr, Los Angeles, CA 90032 and Frank A. Gomez, fgomez2@calstatela.edu, Chemistry and Biochemistry, California State University, Los Angeles, 5151 State University Drive, Los Angeles, CA 90032.
Binding constants between polyethylene glycol (PEG)-derivatized vancomycin (Van from Streptomyces orientalis) species and D-Ala-D-Ala terminus peptides were determined using affinity capillary electrophoresis (ACE). In these experiments a series of Van-PEG (PEG-550, 750, 1100, 2000, 5000, and 8000 g/mol) species were synthesized. Similarly, linked derivatives of teicoplanin from Actinoplanes teicomyceticus were also synthesized and examined. Utilizing ACE, a plug of modified antibiotic and non-interacting standards are injected and electrophoresed. Analysis of the change in the relative migration time ratio (RMTR) of the antibiotic, relative to the non-interacting standards, as a function of the concentration of peptide, yields a value for the binding constant (Kb). These results demonstrate that derivatization of the antibiotics has little effect on the affinity of D-Ala-D-Ala peptide ligands to antibiotics. The findings further prove the versatility of ACE and its ability to estimate binding parameters of ligands to receptors.
 

General Papers
7:00 PM-9:00 PM, Sunday, 10 September 2006 Moscone Center -- Hall D, Poster

Division of Analytical Chemistry

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006