Method development by capillary electrophoresis for analysis of İRGD pepti̇de from in situ gel pharmaceutical preperation and validation

iRGD is a cyclic peptide consisting of 9 amino acids. It is used as an aid in anticancer formulation studies due to its penetration into tumor cells. In this study, a new capillary electrophoresis method was developed to display the iRGD peptide in an in situ gelling formulation. In the study, a capillary column with an effective length of 50 cm and a total length of 58.5 cm and an inner diameter of 75 µm was used. Detection photodiode array (DAD) was provided with the detector and the capillary temperature was set to 20C. At the end of the optimization studies, 20mM phosphate buffer (pH 2.11) and 23 kV potential. The internal standard was tested for iRGD peptide compatibility and olanzapine was determined as the most appropriate internal standard. As a results of analyzes; The mean migration time of olanzapine was 5.82 minutes, and the migration time of iRGD peptide was 7.51 minutes. To demonstrate the validity of the method, linearity, accuracy, precision, stability and robustness tests were performed. As a result of linearity analysis, it was shown that the iRGD peptide is linear between 5.27x10-6 M and 6.33x10-5 M. Percentage of recovery and %BSS values were calculated for precision and accuracy parameters. Compatibility parameters to the system are also shown. As a result, the method was applied to the formulation and the peak of the iRGD peptide was shown in the formulation. This method is the first capillary electrophoresis method developed for the analysis of iRGD peptide.