The de novo protein with grafted biological function: transferring of interferon blast-transforming activity to albebetin

The de novo protein albebetin has been designed recently to form a predetermined tertiary fold that has not yet been observed in natural proteins. An eight amino acid fragment (131–138) of human interferon α2 carrying the blasttransforming activity of the protein was attached to the N-terminus of al...

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Bibliographic Details
Published in:Protein engineering 1996-02, Vol.9 (2), p.195-201
Main Authors: Dolgikh, Dmitry A., Uversky, Vladimir N., Gabrielian, Andrey E., Chemeris, Violetta V., Fedorov, Alexey N., Navolotskaya, Elena V., Zav'yalov, Vladimir P., Kirpichnikov, Michael P.
Format: Article
Language:English
Subjects:
albebetin
Amino Acid Sequence
Animals
Base Sequence
chimeric protein
de novo protein
grafted biological function
Humans
Interferon-alpha - chemistry
Lymphocyte Activation - drug effects
Mice
Molecular Sequence Data
Peptide Fragments - chemistry
Peptide Fragments - metabolism
Protein Engineering
Protein Folding
Protein Structure, Tertiary
Proteins - chemistry
Proteins - genetics
Proteins - metabolism
Receptors, Cell Surface - antagonists & inhibitors
Receptors, Cell Surface - metabolism
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Urea - pharmacology
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Summary:The de novo protein albebetin has been designed recently to form a predetermined tertiary fold that has not yet been observed in natural proteins. An eight amino acid fragment (131–138) of human interferon α2 carrying the blasttransforming activity of the protein was attached to the N-terminus of albebetin next to its initiatory methionine residue. The gene of chimeric protein was expressed in a wheat germ cell-free translation system and synthesized protein was tested for its compactness and stability. Its ability for receptor binding was also studied. We have shown that albebetin with attached octapeptide is practically as compact as natural proteins of corresponding molecular weight and possesses high stability toward the urea-induced unfolding. It binds murine thymocyte receptor at a high affinity and activates the thymocyte blast transformation efficiently at a concentration of 10-11 M.
ISSN:1741-0126
0269-2139
1741-0134
DOI:10.1093/protein/9.2.195