Stanford University's Department of Genetics and several scholars in the Department of Pharmacology have collaborated to develop a new technology for in situ protein engineering that reuses somatic hypermutation, the CRISPR-X, which will help scientists create complex primitives. Genetic mutation library, analysis and perfection of protein engineering.
At present, the protein function is analyzed by directed evolution, and protein engineering research is limited by the overall mutagenesis, or technical problems in DNA library construction. In response to this, this article has developed a new technology for the re-use of somatic hypermutation for in situ protein engineering: CRISPR-X.
The researchers catalyzed the activation of dormant dCas9, which recruited cytosine deaminase (AID) mutations that carry MS2-modified sgRNAs, thereby specifically targeting mutagenic endogenous targets (restricting off-target damage). This allows multiple different point mutation libraries to be generated while targeting multiple genomic loci.
To validate this approach, the researchers mutagenized GFP, screened for spectral shift mutations, such as EGFP, and they also mutated the target of the cancer treatment drug Bortezomib, PSMB5, ​​the only therapeutic malignancy currently approved for marketing. A proteasome inhibitor of tumor that specifically inhibits the chymotrypsin of the 26S proteasome in mammalian cells.
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