Mobility of oligopeptides on normal‐phase silica: Effect of positional isomerism

Abstract

Abstract Isomeric oligopeptides composed of five methionyl residues and one glycyl residue or of five γ‐methyl‐ L ‐glutamyl residues and one glycyl residue all exhibit marked differences in retention on normal‐phase silica. When the glycyl residue is at internal positions of hexa or heptapeptides, the peptide elutes most rapidly form the μPorasil column. Comparison of the effect of positional isomerism on retention in short oligopeptides with the effect on retention of hexamers and heptamers suggests that a change in peptide conformation may be responsible for the change in oligopeptide mobility.

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