期刊
ACS SYNTHETIC BIOLOGY
卷 9, 期 3, 页码 486-493出版社
AMER CHEMICAL SOC
DOI: 10.1021/acssynbio.9b00458
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资金
- Deutsche Forschungsgemeinschaft (DFG) [SCHN 1273/3, GRK 2062]
- Center for Integrated Protein Science Munich (CIPSM) [EXC114]
- Gilead Sciences
- IOCB Research Centre
The site-specific chemical modification of proteins through incorporation of noncanonical amino acids enables diverse applications, such as imaging, probing, and expanding protein functions, as well as to precisely engineer therapeutics. Here we report a general strategy that allows the incorporation of noncanonical amino acids into target proteins using the amber suppression method and their efficient secretion in the biotechnological relevant expression host Bacillus subtilis. This facilitates efficient purification of target proteins directly from the supernatant, followed by their functionalization using click chemistry. We used this strategy to site-specifically introduce norbornene lysine into a single chain antibody and functionalize it with fluorophores for the detection of human target proteins.
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