SUSCEPTIBILITY OF NEUROACTIVE PEPTIDES TO AMINOPEPTIDASE DIGESTION IS RELATED TO MOLECULAR-SIZE

Peptide fragments derived from the NH2-terminus of corticotropin were found to exhibit widely differing degrees of stability to degradation by aminopeptidase M. Corticotropin itself was 135 times more stable than its NH2-terminal pentapeptide, and similar differences in stability were observed with peptides derived from the B-chain of bovine insulin. Enkephalin linked covalently to the A-chain of bovine insulin was at least 100 times more stable than the pentapeptide. The results demonstrate that the molecular size of a peptide is one factor that determines its NH2-terminal stability. © 1979.