The free solution electrophoretic mobility of peptides by a bead modeling methodology

Abstract

A bead modeling methodology, BMM, discussed previously to compute the free solution electrophoretic mobility of peptides [H. Pei, Y. Xin, S.A. Allison, J. Sep. Sci. 31 (2008) 554–564], is generalized to avoid the approximation of orientationally preaveraging hydrodynamic interaction. In general, peptide mobilities computed without preaveraging are lower by about 2%. The BMM is then used to study the free solution electrophoretic mobility of several insect oostatic peptides reported previously in a variety of different buffer systems ranging in pH from 2.25 to 8.1 [V. Solinova, V. Kasicka, D. Koval, J. Hlavacek, Electrophoresis, 25 (2004) 2299–2308]. With minor adjustment of the intrinsic pK a0 of the N-terminal peptide, good agreement between modeling and experiment is achieved for peptide models with random secondary structures in the entire pH range. Model mobilities of these peptides appear to be relatively insensitive to the assumed secondary structure.