Side reactions in peptide synthesis. II. Formation of succinimide derivatives from aspartyl residues.
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Biomedical subjects
Publications and source records attributed to M Bodanszky.
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A structure (the disulfide form of cyclo-D-cysteinyl-L-valyl-D-cysteinyl-D-leucyl-L-isoleucyl), previously proposed for malformin A, was reexamined. On the basis of chemical degradations, a different structure (the disulfide form of cyclo-D-cysteinyl-D-cysteinyl-L-valyl-D-leucyl-L-isoleucyl) was established. Accordingly, a compound with this structure was synthesized and was found to be identical with malformin A. The synthetic product causes curvatures on corn roots; maximum effect was seen at a concentration of 0.1 mug/ml, the optimal concentration for malformin A.
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An octacosapeptide with the entire sequence proposed for the newly isolated vasoactive intestinal polypeptide was synthesized and had the expected biological properties. Synthetic peptides corresponding to the C-terminal hendeca-, tetradeca-, pentadeca-, and docosapeptide sequences of the vasoactive intestinal polypeptide showed activities that increased with increasing chain length.
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