25055-82-7Relevant articles and documents
Base-mediated one-pot synthesis of aliphatic diazirines for photoaffinity labeling
Wang, Lei,Tachrim, Zetryana Puteri,Kurokawa, Natsumi,Ohashi, Fumina,Sakihama, Yasuko,Hashidoko, Yasuyuki,Hashimoto, Makoto
, (2017)
Aliphatic diazirines have been widely used as prominent photophores for photoaffinity labeling owing to their relatively small size which can reduce the steric effect on the natural interaction between ligands and proteins. Based on our continuous efforts
Genetically Encoded 2-Aryl-5-carboxytetrazoles for Site-Selective Protein Photo-Cross-Linking
Tian, Yulin,Jacinto, Marco Paolo,Zeng, Yu,Yu, Zhipeng,Qu, Jun,Liu, Wenshe R.,Lin, Qing
, p. 6078 - 6081 (2017)
The genetically encoded photo-cross-linkers promise to offer a temporally controlled tool to map transient and dynamic protein-protein interaction complexes in living cells. Here we report the synthesis of a panel of 2-aryl-5-carboxytetrazole-lysine analogs (ACTKs) and their site-specific incorporation into proteins via amber codon suppression in Escherichia coli and mammalian cells. Among five ACTKs investigated, N-methylpyrroletetrazole-lysine (mPyTK) was found to give robust and site-selective photo-cross-linking reactivity in E. coli when placed at an appropriate site at the protein interaction interface. A comparison study indicated that mPyTK exhibits higher photo-cross-linking efficiency than a diazirine-based photo-cross-linker, AbK, when placed at the same location of the interaction interface in vitro. When mPyTK was introduced into the adapter protein Grb2, it enabled the photocapture of EGFR in a stimulus-dependent manner. The design of mPyTK along with the identification of its cognate aminoacyl-tRNA synthetase makes it possible to map transient protein-protein interactions and their interfaces in living cells.
Substrate Profiling of Mitochondrial Caseinolytic Protease P via a Site-Specific Photocrosslinking Approach
Gronauer, Thomas F.,Lang, Kathrin,Nast-Kolb, Timon,Nguyen, Tuan-Anh,Sieber, Stephan A.
, (2022/01/20)
Approaches for profiling protease substrates are critical for defining protease functions, but remain challenging tasks. We combine genetic code expansion, photocrosslinking and proteomics to identify substrates of the mitochondrial (mt) human caseinolytic protease P (hClpP). Site-specific incorporation of the diazirine-bearing amino acid DiazK into the inner proteolytic chamber of hClpP, followed by UV-irradiation of cells, allows to covalently trap substrate proteins of hClpP and to substantiate hClpP's major involvement in maintaining overall mt homeostasis. In addition to confirming many of the previously annotated hClpP substrates, our approach adds a diverse set of new proteins to the hClpP interactome. Importantly, our workflow allows identifying substrate dynamics upon application of external cues in an unbiased manner. Identification of unique hClpP-substrate proteins upon induction of mt oxidative stress, suggests that hClpP counteracts oxidative stress by processing of proteins that are involved in respiratory chain complex synthesis and maturation as well as in catabolic pathways.
Non-natural amino acid and application thereof in protein site-specific modification and protein interaction
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Paragraph 0160-0162, (2021/02/13)
The invention relates to a non-natural amino acid compound represented by a general formula (I) and a preparation method thereof, and applications of the non-natural amino acid compound in fixed-pointmodification of bio-macro-molecular proteins, protein i
NOVEL MOLECULES FOR TARGETING RIBOSOMES AND RIBOSOME-INTERACTING PROTEINS, AND USES THEREOF
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Page/Page column 35-36, (2020/02/06)
Molecule having the structural formula (I): (I) for use as targeting probe of translating ribosomes and ribosome-interacting proteins.
