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Studies on the relationship between structure and electrophoretic mobility of α-helical and β-sheet peptides using capillary zone electrophoresis

1999; Elsevier BV; Volume: 857; Issue: 1-2 Linguagem: Inglês

10.1016/s0021-9673(99)00768-2

1873-3778

Balvant R. Sitaram, Hooi Hong Keah, Milton T. W. Hearn,

Spectroscopy and Quantum Chemical Studies

The electrophoretic behaviour of a series of 33 different synthetic peptides has been investigated using free solution high-performance capillary zonal electrophoretic (HPCZE) methods. The dependency of the electrophoretic mobility, μem, on the peptide charge, q, and on the charge-to-size ratio parameter, ζ, determined according to several electromobility models, have been examined. Significant divergences from linearity in the μem vs. q or the μem vs. ζ plots were noted for several peptides, possibly due to the proclivity of specific arrangements of their amino acid sequences to assume preferred α-helical or β-sheet conformational features rather than random coil structures under the HPCZE conditions. These results provide further demonstration of the facility of HPCZE procedures to probe the effects of compositional, sequential and conformational differences of closely-related peptides and their consequences on their physicochemical behaviour in solution.