| | 1 | Author
| Anders Ljungqvist, Karl Folkers | Requires cookie* | | | Title
| Study of Hydrogenolytic Cleavage of Peptide-Resin Benzyl Ester Bonds for Synthesis of Protected Fragments of the Human Leukocyte Interferon  | | | | Abstract
| Three Boc-protected fragments of the human leukocyte interferon, LeIFA, have been synthesized: I, BOC LeIFA (99-105) (BOC-Val-Ile-Gln-Gly-Val-Gly-Val); II, BOC LeIFA (116-119) (BOC-Ile-Leu-Ala-Val); III, BOC LeIFA (123-126) (BOC-Phe-Gln-Arg(Tos)-Ile). The presence of the Boc-group was desired so that these peptides could serve as intermediates in fragment condensation toward larger segments of interferon. To achieve these intermediates, a study was desirable on three methods of cleavage of the benzyl ester-polymer bonds. It was found that hydrogenolysis with hydrogen and palla-dium generated in situ was distinctly superior to transfer hydrogenation with ammonium formate or cyclohexene. An effective swelling of the peptide-resin to allow penetration of palladium acetate into the matrix and mobility of the peptide chains on the resin to expose the benzyl ester bond to hydrogenolysis appear to be essential conditions for the best cleavage. | | | |
Reference
| Z. Naturforsch. 38b, 1022—1024 (1983); received May 2 1983 | | | |
Published
| 1983 | | | |
Keywords
| Interferon, Peptide Synthesis, Hydrogenation, Palladium Black, Conformation | | | |
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| default:Reihe_B/38/ZNB-1983-38b-1022.pdf | | | | Identifier
| ZNB-1983-38b-1022 | | | | Volume
| 38 | |
| 2 | Author
| Anders Ljungqvist, Karl Folkers+ | Requires cookie* | | | Title
| Synthesis of a Combined Fragment of Interferon, AeHuIFN a A(30-43)-(123-137)-NH2 Interferon May not be a Sychnologieal Peptide * AeHuIFN a A( 30-43)-( 123-137)-NH2, Ac-Leu-Lys-Asp-Arg-His-Asp-Phe-Gly-Phe- Pro-Gln-Glu-Glu-Phe-Phe-Gln-Arg-Ile-Thr-Leu-Tyr-Leu-Lys-Glu-Lys-Lys-Tyr-Ser- Pro-NH2 was | | | | Abstract
| synthesized toward encompassing the "active site" of the interferons. The design of this 29-amino acid peptide was based on considerations of homology between the different interferons and on combining two regions of interferons, and on known and predicted structural features. The peptide was characterized by amino acid analysis, thin layer chromatography in several systems, and by HPLC. As tested, the peptide neither showed antiviral activity nor blocked antiviral activity of interferon, indicating that the active site was not encompassed or that interferon may not be a sychnologieal peptide. | | | |
Reference
| Z. Naturforsch. 38b, 1249—1252 (1983); received June 24 1983 | | | |
Published
| 1983 | | | |
Keywords
| Interferon, Peptide Synthesis, Antiviral Activity, Synthetic Fragment, Active Site | | | |
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| default:Reihe_B/38/ZNB-1983-38b-1249.pdf | | | | Identifier
| ZNB-1983-38b-1249 | | | | Volume
| 38 | |
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