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Total chemical synthesis of human interferon alpha-2b via native chemical ligation
- Source :
- Journal of peptide science : an official publication of the European Peptide Society. 21(7)
- Publication Year :
- 2014
-
Abstract
- Interferon-alpha (IFNα) is a cytokine that orchestrates innate and adaptive immune responses, and potently inhibits proliferation of normal and tumor cells. These properties have warranted the use of IFNα in clinical practice for the treatment of several viral infections and malignancies. However, over-expression of IFNα leads to immunopathology observed in the context of chronic viral infections and autoimmune conditions. Thus, it is desirable to develop therapeutic approaches that aim at suppressing excessive IFNα production. To that end, artificial evolution of peptides from phage display libraries represents a strategy that seeks to disrupt the interaction between IFNα and its cell surface receptor, and thus inhibit the ensuing biological effects. Mirror-image phage display that screens peptide libraries against the D-enantiomer is particularly attractive because it allows for identification of proteolysis-resistant D-peptide inhibitors. This approach, however, relies on the availability of chemically synthesized D-IFNα composed entirely of D-amino acids. Here we describe the synthesis and biological properties of IFNα2b of 165 amino acid residues produced by native chemical ligation, which represents an important first step toward the discovery of D-peptide antagonists with potential therapeutic applications.
- Subjects :
- Models, Molecular
Protein Folding
T-Lymphocytes
Molecular Sequence Data
Primary Cell Culture
Interferon-alpha
Epithelial Cells
Stereoisomerism
Interferon alpha-2
Recombinant Proteins
Article
Peptide Library
Cell Line, Tumor
Humans
Amino Acid Sequence
Disulfides
Encephalomyocarditis virus
Peptides
Solid-Phase Synthesis Techniques
Cell Proliferation
Subjects
Details
- ISSN :
- 10991387
- Volume :
- 21
- Issue :
- 7
- Database :
- OpenAIRE
- Journal :
- Journal of peptide science : an official publication of the European Peptide Society
- Accession number :
- edsair.pmid..........ae9687b42cbb9ff5223a3b9bc6b73284