Bioorganic synthesis of a recombinant HIV-1 fusion inhibitor, SC35EK, with an N-terminal pyroglutamate capping group
| Autor: | Hiroaki Ohno, Shinya Oishi, Tomoko Kurose, Nobutaka Fujii, Hiroko Tsutsumi, Kazuki Izumi, Kazumi Kajiwara, Kentaro Watanabe, Eiichi Kodama, Masao Matsuoka, Yoji Hata, Rei Tokiwa |
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| Rok vydání: | 2009 |
| Předmět: |
Spectrometry
Mass Electrospray Ionization Stereochemistry Clinical Biochemistry Pyroglutamate Homoserine Pharmaceutical Science Peptide Cleavage (embryo) Biochemistry Chemical synthesis law.invention Mice chemistry.chemical_compound Blood serum 4-Butyrolactone HIV Fusion Inhibitors law Drug Discovery Animals Humans Anti-HIV peptide Molecular Biology Bond cleavage Cell Proliferation Fusion inhibitor chemistry.chemical_classification Chemistry Circular Dichroism Organic Chemistry HIV Recombinant Proteins Pyrrolidonecarboxylic Acid HIV-1 Recombinant DNA Molecular Medicine Lactone HeLa Cells |
| Zdroj: | Bioorganic & Medicinal Chemistry. 17:7964-7970 |
| ISSN: | 0968-0896 |
| DOI: | 10.1016/j.bmc.2009.10.017 |
| Popis: | The bioorganic synthesis of an end-capped anti-HIV peptide from a recombinant protein was investigated. Cyanogen bromide-mediated cleavage of two Met-Gln sites across the target anti-HIV sequence generated an HIV-1 fusion inhibitor (SC35EK) analog bearing an N-terminal pyroglutamate (pGlu) residue and a C-terminal homoserine lactone (Hsl) residue. The end-capped peptide, pGlu-SC35EK-Hsl, had similar bioactivity and biophysical properties to the parent peptide, and an improved resistance to peptidase-mediated degradation was observed compared with the non-end-capped peptide obtained using standard recombinant technology. |
| Databáze: | OpenAIRE |
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