Synthesis and biological properties of chimeric interferon-α2b peptides
| Autor: | Viviana C. Blank, Leonor P. Roguin, Clara Peña, Veronica Julieta Marino |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Protein Conformation
Physiology Stereochemistry medicine.medical_treatment Molecular Sequence Data Peptide Interferon alpha-2 Binding Competitive Peptides Cyclic Biochemistry law.invention Cellular and Molecular Neuroscience chemistry.chemical_compound Endocrinology Protein structure Biosynthesis law medicine Humans Amino Acid Sequence Receptor Peptide sequence Cells Cultured Cell Proliferation Receptors Interferon chemistry.chemical_classification Cell growth Interferon-alpha Peptide Fragments Recombinant Proteins Cytokine chemistry Recombinant DNA |
| Zdroj: | Peptides. 26:1144-1149 |
| ISSN: | 0196-9781 |
| DOI: | 10.1016/j.peptides.2005.01.004 |
| Popis: | We have previously reported the antiproliferative activity of synthetic sequences 29-35 and 122-139 of the interferon-alpha2b (IFN-alpha2b), both probably representing a common receptor recognition domain. In the search of new peptidic agonists, we designed and synthesized the linear peptide (Gly)2-122-137-Gly138-Gly29-30-35-(Gly)2, in which Gly residues replaced the 138 and 29 Cys bound through a disulfide bridge in the native cytokine. Additionally, a cyclic analog was obtained by reaction of the N- and C-terminal ends of the linear fragment. Thus, the distance that separates residues 122 and 35 in the crystalline structure of the IFN-alpha2b was maintained through a (Gly)4 bridge. When the influence of chimeric peptides on the proliferation of WISH cells was studied, it was shown that both derivatives significantly diminished cell growth. A more evident inhibitory effect on (125)I-IFN-alpha2b binding to WISH cell-membrane receptors was observed for both peptides. Results indicated that chimeric IFN-alpha2b peptides behaved as partial agonists of the IFN-alpha2b molecule and may be of interest for drug design purposes. |
| Databáze: | OpenAIRE |
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