Tactics for simplification of purification process in the solid phase peptide synthesis.

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Abstract
These tactics depend primarily on coupling of a highly polar compound, as a highly polar handle in the purification process, with the terminal amino group of the desired sequence assembled on a solid support. Lysine was used as the highly polar compound in this study. All protecting groups labile towards HF were removed as usual and the resulting crude peptide was purified through a CM-cellulose column. The amino terminal lysine residue was removed by Edman degradation to obtain the desired peptide. This permitted the syntheses of peptide fragments of the B chain of human insulin, H-Gly-Phe-Phe-Tyr-Thr-Pro-Lys(Tfa)-Thr-OH [Lys(Tfa) is the trifluoroacetylated derivative] and H-Gly-Ser-His-Leu-Val-OH, with a simple purification process in good yield and in high purity.