Modeling the electrophoresis of oligoglycines.
The electrophoretic mobility of low molecular mass oligoglycines is examined in this study using a "coarse-grained" bead modeling methodology [Pei, H., Allison, S. A., J. Chromatogr. A 2009, 1216, 1908-1916]. The advantage of focusing on these peptides is that their charge state is well known [Plasson, R., Cottet, H., Anal. Chem. 2006, 78, 5394-5402] and extensive electrophoretic mobility data are also available in different buffers [Survay, M. A., Goodall, D. M., Wren, S. A. C., Rowe, R. C., J. Chromatogr. A 1996, 741, 99-113] and over a broad range of temperatures [Plasson, R., Cottet, H., Anal Chem. 2005, 77, 6047-6054]. Except for assumptions about peptide secondary structure, the B model has no adjustable parameters. It is concluded that the oligoglycines adopt a random configuration at high temperature (50 degrees C and higher), but more compact conformations at lower temperature. It is proposed that triglycine through pentaglycine adopt compact cyclic structures at low temperature (up to about 25 degrees C) in aqueous solution. At 25 degrees C, buffer interactions are also examined and may or may not influence peptide conformation depending on the buffer species. In a borate buffer at high pH, the mobility data are consistent with complex formation between the oligoglycine and borate anion.
Allison
Stuart A
SA
Department of Chemistry, Georgia State University, Atlanta, GA 30302-4098, USA sallison@gsu.edu
Pei
Hongxia
H
Twahir
Umar
U
Wu
Hengfu
H
Cottet
Herve
H
D019075:Electrophoresis, Capillary; D005998:Glycine / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D008956:Models, Chemical; D009842:Oligopeptides / Q000302:isolation & purification*; D011487:Protein Conformation; D013696:Temperature
D009842:Oligopeptides; D005998:Glycine