Separation of cis/trans isomers of a prolyl peptide bond by capillary zone electrophoresis

作者：Sylke Meyer, Andreas Jabs, Mike Schutkowski, Gunter S. Fischer · 发表于：Electrophoresis · 年份：1994 · DOI：10.1002/elps.11501501174 · 被引用次数：19 · 研究领域：Protein Structure and Dynamics、Chemical Synthesis and Analysis、Enzyme Structure and Function

On capillary electrophoresis of the chemically pure thioxo peptide Ala-Phe-psi[CS-N]-Pro-Phe-4-nitroanilide a peak splitting was observed at a capillary temperature of 25 degrees C. By contrast, the oxo peptide analogue exhibits a single, sharp peak under these conditions. Both peaks of the thioxo compound coincided gradually when the temperature was increased to 60 degrees C. Peak fusion was reverted by cooling down the heated sample. This behavior could be attributed to the electrophoresis-mediated separation of the cis/trans prolyl bond isomers of the thioxo peptide, allowing data of this conformational equilibrium to be determined. Derived from computational data about molecular volume and the hydration energy of low-energy cis and trans isomeric structures, the more rapid migration of the cis form in comparison to trans may be explained by structural parameters.