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Immunochemical and biological properties of synthetic peptide fragments from the amino acid sequence 124–144 of the human leukocyte interferon α2
A. F. Shevalier, V. V. Samukov, V. I. Ofitserov, V.V. Kalashnikov, G. A. Mizenko, A. A. Kolokoltsov
Ail-Union Research Institute of Molecular Biology, Koltsovo, Novosibirsk Region
Abstract: Three peptides corresponding to the sequences 124–144, 124–138, 129–144 of the human leukocyte interferon α2 (IFN-α2) were synthesized. The synthesis was performed by DCC-HOBT coupling of protected peptide segments in solution. The segments were obtained by the active ester coupling methodology using base-labile 2-[4-(phenylazoben-zyl)sulfonyl]ethyl (Pse) group as carboxyterminal protection. After complete deprotec-tion with 1 M methanesulphonic acid in trifluoroacetic acid – thioanisol – m-cresol mixture the peptides were purified by reversed-phase chromatography. The studies of interaction of the peptides with rabbit antiserum against IFN-α2 revealed at least one minor antigenic determinant within the 124–144 region of IFN-α2 amino acid sequence. Rabbit antisera developed against peptides 124–138 and 129–144 showed ability of binding recombinant IFN-α2 and neutralizing its antiviral activity. Free peptides or their conjugates with bovine serum albumine did not display antiviral activity, neither could they inhibit the activity of IFN-α2.
Russian Journal of Bioorganic Chemistry 1990, 16 (7):916-925