Synthesis of peptides analogous to the N-terminal eicosapeptide of ribonuclease A. Part IV. Synthesis of the enzymatically active Orn10 and Orn10, Glu11-eicosapeptides
- 1 January 1967
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society C: Organic
- p. 606-610
- https://doi.org/10.1039/j39670000606
Abstract
The syntheses of two analogous N-terminal eicosapeptides of the bovine pancreatic ribonuclease A, the Orn10-and the Orn10- Glu11-S-peptides, are described. N α N ε -Di-t-butoxycarbonyl-L-lysyl-γ-t-butyl-L-glutamyl-L-threonyl-L-alanyl-L-alanyl-L-alanine azide was condensed with Nε-t-butoxycarbonyl-L-lysyl-L-phenylalanyl-γ-t-butyl-L-glutamyl-Nδ-t-butoxycarbonyl-L-ornithyl-L-glutaminyl-L-histidine methyl ester or with Nε-t-butoxycarbonyl-L-lysyl-L-phenylalanyl-γ-t-butyl-L-glutamyl-Nδ-t-butoxycarbonyl-L-ornithyl-γ-t-butyl-L-glutamyl-L-histidine methyl ester. The hydrazides of the dodecapeptide esters were condensed, by an azide coupling step, with the C-terminal octapeptide, L-methionyl-L-aspartyl-L-seryl-L-seryl-L-threonyl-L-seryl-L-alanyl-L-alanine. The resulting eicosapeptides, after treatment with trifluoroacetic acid, were purified by chromatography on Amberlite C.G. 50, desalted on Sephadex G. 25 and lyophilised. The synthetic peptides, after recombination with S-protein in different ratios, were able to restore 37–88% of the activity of the RNase S′, with yeast ribonucleic acid as substrate.Keywords
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