Peptide-ligand interactions in open-tubular capillary columns covalently modified with porphyrins

YONE A; CARBALLO R; GRELA D; GARCÍA MB; REZZANO IN; VIZIOLI NM

Miami

Simposio; 17th Symposium on Biomedical, Biopharmaceutical and Industrial Applications of Capillary Electrophoresis and Microchip Technology; 2011

Porphyrins, a group of naturally occurring macrocyclic compounds, have a recognized number of chemical characteristics that can be exploited in analytical chemistry. Porphyrins and their derivatives present different binding capabilities necessary for specific interactions. In this work, the inner surface of fused-silica capillaries has been covalently modified with different porphyrins (deuteroporphyrin, complexes of deuteroporphyrin with metal ions Fe(III), Cu(II), Zn(II), Ni(II), and Cu(II)- meso–tetra (carboxyphenyl) porphyrin) and it was applied for the separation of biologically active peptides by open-tubular capillary electrochromatography. Changes in the effective electrophoretic mobility of peptides were studied concerning porphyrin central metal atom, attachment geometry and the presence of coordinating or aromatic amino acid residues in the peptide sequence. The results showed that differences in metal-core on the porphyrin and the spatial conformation of attached porphyrin, result in changes in the analyte interaction with the stationary phase.