AI Article Synopsis
- The biotin-streptavidin interaction is an extremely strong binding system used for protein studies.
- The study explores incorporating biotin and 2-iminobiotin, which are derived from noncanonical amino acids, into proteins for better purification and analysis.
- This method allows for specific isolation of proteins like RecA and can be applied to mammalian cells, providing a versatile tool for research in protein interactions and drug design.
Article Abstract
The biotin-streptavidin interaction is among the strongest known in nature. Herein, the site-directed incorporation of biotin and 2-iminobiotin composed of noncanonical amino acids (ncAAs) into proteins is reported. 2-Iminobiotin lysine was employed for protein purification based on the pH-dependent dissociation constant to streptavidin. By using the high-affinity binding of biotin lysine, the bacterial protein RecA could be specifically isolated and its interaction partners analyzed. Furthermore, the biotinylation approach was successfully transferred to mammalian cells. Stringent control over the biotinylation site and the tunable affinity between ncAAs and streptavidin of the different biotin analogues make this approach an attractive tool for protein interaction studies, protein immobilization, and the generation of well-defined protein-drug conjugates.
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| http://dx.doi.org/10.1002/cbic.201900015 | DOI Listing |
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