Synthesis is described for the N‐o‐nitrophenylsulfenylheptapeptide tert‐butoxycarbonylhydrazide corresponding to positions 17–23 of the amino acid sequence of baker's yeast iso‐1‐cytochrome c. Moreover a new method of selective removal of the S‐acetamidomethyl group for analytical and preparative purpose is reported.

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSynthesis of peptide analogs of the N-terminal eicosapeptide sequence of ribonuclease A. XIII. Synthesis of des-Lys7-[Orn10]- and des-Phe8-[Orn10]-S-peptidesRaniero Rocchi, Fernando Marchiori, Luigi Moroder, Gianfranco Borin, and Ernesto ScoffoneCite this: J. Am. Chem. Soc. 1969, 91, 14, 3927–3931Publication Date (Print):July 1, 1969Publication History Published online1 May 2002Published inissue 1 July 1969https://pubs.acs.org/doi/10.1021/ja01042a041https://doi.org/10.1021/ja01042a041research-articleACS PublicationsRequest reuse permissionsArticle Views25Altmetric-Citations15LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSynthesis of peptide analogs of the N-terminal eicosapeptide sequence of ribonuclease A. XII. Synthesis of des-Lys1-[Orn10]-, and des-Lys1,Glu2,Thr3-[Orn10]-S-peptides1,2Luigi Moroder, Fernando Marchiori, Raniero Rocchi, Angelo Fontana, and Ernesto ScoffoneCite this: J. Am. Chem. Soc. 1969, 91, 14, 3921–3926Publication Date (Print):July 1, 1969Publication History Published online1 May 2002Published inissue 1 July 1969https://pubs.acs.org/doi/10.1021/ja01042a040https://doi.org/10.1021/ja01042a040research-articleACS PublicationsRequest reuse permissionsArticle Views28Altmetric-Citations14LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

Synthesis is described of the Orn10-dodecapeptide analogous to the 1–12 N-terminal sequence of the bovine pancreatic ribonuclease A. The hexapeptide NαNε-di-t-butoxycarbonyl-L-lysyl-γ-t-butyl-L-glutamyl-L-threonyl-L-alanyl-L-alanyl-L-alanine ethyl ester (positions 1–6) was obtained either by a stepwise process starting from the C-terminal residue, or by the azide procedure by coupling the NαNε-di-t-butoxycarbonyl-L-lysyl-γ-t-butyl-L-glutamyl-L-threonine hydrazide with the L-alanyl-L-alanyl-L-alanine ethyl ester.This hexapeptide ester was transformed to the corresponding azide and 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 to give the protected Orn10-dodecapeptide ester.

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.