A Model System for Studying Peptide Synthesis on Polymeric Supports by Ion Exchange Chromatography

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Abstract
From a cation exchange resin the eight peptide intermediates obtained during the synthesis of the deamido form of the calcitonine M sequence 24–32 Gln-Thr-Ala-lle-Gly-Val-Gly-Ala-Pro are eluted by a gradient of pyridine acetate buffers according to size. The peptide with highest molecular weight is eluted first. This makes the synthesis of this sequence suitable as a model system for studying various parameters of peptide synthesis on solid supports. Due to the sensitivity of the chromatographic system the model is particularly useful for the determination of coupling yields. Analytical procedures are described which allow the determination of coupling yields with a limit of sensitivity at about 0.05% unreacted peptide. A detailed analysis of a synthesis of the pentapeptide Gly-Val-Gly-Ala-Pro and a study of the necessity of the side chain protection for threonine are described as examples of application of the model system.

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