Direct protein-protein conjugation by genetically introducing bioorthogonal functional groups into proteins

Proteins often function as complex structures in conjunction with other proteins. Because these complex structures are essential for sophisticated functions, developing protein-protein conjugates has gained research interest. In this study, site-specific protein-protein conjugation was performed by genetically incorporating an azide-containing amino acid into one protein and a bicyclononyne (BCN)-containing amino acid into the other. Three to four sites in each of the proteins were tested for conjugation efficiency, and three combinations showed excellent conjugation efficiency. The genetic incorporation of unnatural amino acids (UAAs) is technically simple and produces the mutant protein in high yield. In addition, the conjugation reaction can be conducted by simple mixing, and does not require additional reagents or linker molecules. Therefore, this method may prove very useful for generating protein-protein conjugates and protein complexes of biochemical significance. (C) 2016 Published by Elsevier Ltd
Publisher
PERGAMON-ELSEVIER SCIENCE LTD
Issue Date
2016-11
Language
ENG
Keywords

FREE CLICK CHEMISTRY; ESCHERICHIA-COLI; IN-VIVO; TRANS-CYCLOOCTENES; ALDEHYDE TAG; AMINO-ACID; SITE; CODE; LIGATION; FUSIONS

Citation

BIOORGANIC & MEDICINAL CHEMISTRY, v.24, no.22, pp.5816 - 5822

ISSN
0968-0896
DOI
10.1016/j.bmc.2016.09.035
URI
http://hdl.handle.net/10203/214814
Appears in Collection
BS-Journal Papers(저널논문)
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