[A14-Phenylalanine]Insulin: A New Synthetic Analogue

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Abstract
An analog of porcine insulin, which differs from the native molecule in that the amino acid residue A 14-Tyr is replaced by Phe, was synthesized. The [PheA14]A chain was synthesized by the fragment condensation method and purified as tetra-S-sulfonate by ion-exchange chromatography on DEAE-cellulose at pH 5.6. Conversion of the tetra-S-sulfonate A chain to the sulfhydryl form and combination with native porcine sulfhydryl B chain gave the [PheA14]insulin, which was purified by gel filtration and ion-exchange chromatorgraphy on DEAE-cellulose. The biological activity of this analog was 96 .+-. 6% as measured by the rat epididymal adipocytes. A14-Tyr is not essential for the biological activity of the hormone.