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Therapeutic applications of genetic code expansion

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Synthetic and Systems Biotechnology 2018年第3期3卷 150-158页

作者： Yujia Huang Tao Liu State Key Laboratory of Natural and Biomimetic Drugs School of Pharmaceutical SciencesPeking UniversityBeijing100191China

In nature,a limited,conservative set of amino acids are utilized to synthesize *** code expansion technique reassigns codons and incorporates noncanonical amino acids(ncAAs)through orthogonal aminoacyltRNA synthetase(aaRS)/tRNA *** past decade has witnessed the rapid growth in diversity and scope for therapeutic applications of this ***,we provided an update on the recent progress using genetic code expansion in the following areas:antibody-drug conjugates(ADCs),bispecific antibodies(BsAb),immunotherapies,long-lasting protein therapeutics,biosynthesized peptides,engineered viruses and cells,as well as other therapeutic related applications,where the technique was used to elucidate the mechanisms of biotherapeutics and drug targets.

关键词： genetic code expansion Noncanonical amino acids Biotherapeutics Antibody-drug conjugates Live-attenuated vaccines

Functional Photoactive Protein Synthesis Using genetic code expansion

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Functional Photoactive Protein Synthesis Using Genetic Code ...

中国化学会-生物物理化学专业委员会第四届全国生物物理化学会议

作者：王江云 Institute of Biophysics Chinese Academy of Sciences

The ability to selectively modify proteins with fluorescent probes has greatly facilitated both in vitro and in vivo studies of protein structure and function. Here we report that genetic code expansion can significantly improve our ability to visualize the proteome. We are the first to report the genetic incorporation of a fluorescent amino acid(Cou AA) into proteins in E. coli in response to the amber stop codon. Recently, we have successfully incorporated unnatural amino acids bearing cyclopropene or tetrazole functional groups. Through photoclick reaction, we can site-specifically attach any biophysical probe to a specific site of a target protein in vivo. The photoclick reaction has the following advantages: its fast rate(50 M-1 s-1) allows for efficient protein labeling in one minute;spatiotemporal control by laser. We are now applying this technology for super-resolution imaging, post-translational modification sensing, as well as imaging in living plants. We have significantly expanded the function of fluorescent proteins through the genetic incorporation of metal-chelating unnatural amino acids. In recent works, we have bestowed GFP with metal-sensing function, and emission spectra in the infrared range. We are now using these new GFP variant for deep-tissue imaging. Most recently, we have designed an acid and Mn(Ⅲ) turn-on fluorescent protein sensor based on genetic code expansion. We are currently using this method for protein and virus endocytosis. These unpublished works will be discussed in the conference.

关键词： genetic code expansion photoclick

Functional Photoactive Protein Synthesis Using genetic code expansion

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Functional Photoactive Protein Synthesis Using Genetic Code ...

中国化学会第30届学术年会-第二十七分会：光化学

作者： Jiangyun Wang Institute of Biophysics Chinese Academy of Sciences

The ability to selectively modify proteins with fluorescent probes has greatly facilitated both in vitro and in vivo studies of protein structure and function. Here we report that genetic code expansion can significantly improve our ability to visualize the proteome. We are the first to report the genetic incorporation of a fluorescent amino acid（Cou AA） into proteins in E. coli in response to the amber stop codon. Recently, we have successfully incorporated unnatural amino acids bearing cyclopropene or tetrazole functional groups. Through photoclick reaction, we can site-specifically attach any biophysical probe to a specific site of a target protein in vivo. The photoclick reaction has the following advantages: its fast rate（50 M-1s-1） allows for efficient protein labeling in one minute;spatiotemporal control by laser. We are now applying this technology for super-resolution imaging, post-translational modification sensing, as well as imaging in living plants. We have significantly expanded the function of fluorescent proteins through the genetic incorporation of metal-chelating unnatural amino acids. In recent works, we have bestowed GFP with metal-sensing function, and emission spectra in the infrared range. We are now using these new GFP variant for deep-tissue imaging. Most recently, we have designed an acid and Mn（III） turn-on fluorescent protein sensor based on genetic code expansion. We are currently using this method for protein and virus endocytosis. These unpublished works will be discussed in the conference.

关键词： genetic code expansion photoclick

A DNA Force Circuit for Exploring Protein-Protein Interactions at the Single-Molecule Level

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Chinese Journal of Chemistry 2024年第13期42卷 1456-1464页

作者： Kangkang Ma Luoan Xiong Zhuofei Wang Xin Hu Lihua Qu Xuetong Zhao Yao Li Zhongbo Yu State Key Laboratory of Medicinal Chemical Biology Frontiers Science Center for Cell Responsesand College of PharmacyNankai University38 Tongyan RoadTianjin 300350China School of Physics and Key Laboratory of Functional Polymer Materials of Ministry of Education Nankai Universityand Collaborative Innovation Center of Chemical Science and EngineeringTianjin 300071China

Protein-protein interactions(PPls)play a crucial role in drug discovery and disease ***,the development of effective drugs targeting PPls remains challenging due to limited methodologies for probing their spatiotemporal ***,we propose a single-molecule approach using a unique force circuit to investigate Ppl dynamics and anisotropy under mechanical *** conventional techniques,this approach enables the manipulation and real-time monitoring of individual proteins at specific amino acids with defined geometry,offering insights into molecular mechanisms at the single-molecule *** DNA force circuit was constructed using click chemistry conjugation methods and genetic code expansion techniques,facilitating orthogonal conjugation between proteins and nucleic *** SET domain of the MLL1 protein and the tail of histone H3 were used as a model system to demonstrate the application of the DNA force *** the use of atomic force microscopy and magnetic tweezers,optimized assembly procedures were *** DNA force circuit provides an exceptional platform for studying the anisotropy of PPis and holds promise for advancing drug discovery research targeted at PPIs.

关键词： Single-molecule studies Protein-protein interactions Click chemistry genetic code expansion Molecular dynamics

Site-specific protein modification by genetic encoded disulfide compatible thiols

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Chinese Chemical Letters 2020年第1期31卷 163-166页

作者： Xinyu Ling Heqi Chen Wei Zheng Liying Chang Yong Wang Tao Liu State Key Laboratory of Natural and Biomimetic Drugs School of Pharmaceutical SciencesPeking University

Cysteine chemistry provides a low cost and convenient way for site-specific protein ***,recombinant expression of disulfide bonding containing protein with unpaired cysteine is technically challenging and the resulting protein often suffers from significantly reduced yield and *** we used genetic code expansion technique to introduce a surface exposed self-paired dithiol functional group into proteins,which can be selectively reduced to afford active *** compounds containing self-paired disulfides were synthesized,and their genetic incorporations were validated using green fluorescent proteins(GFP).The compatibility of these self-paired di-thiols with natural disulfide bond was demonstrated using antibody fragment to afford site-specifically labeled *** work provides another valuable building block into the chemical tool-box for site-specific labeling of proteins containing internal disulfides.

关键词： Cysteine chemistry genetic code expansion Protein modification Biorthogonal chemistry Disulfide bond

Expanding the genetic code

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Expanding the Genetic Code

第二届全国“跨学科蛋白质研究”学术讨论会

作者：王江云 Institute of Biophysics Chinese Academy of Sciences

By engineering t-RNA and t-RNA synthetase,I have first genetically incorporated fluorescent amino acids in *** are now using these environmentally sensitive fluorescent amino acids to probe enzyme mechanism,protein folding,and protein-protein ***,because the fluorescent amino acids are pH sensitive,they are incorporated into cytokines to probe the kinetics of cytokine endocytosis process.

关键词： genetic code expansion unnatural amino acids

Expanding the genetic code of Pseudomonas aeruginosa

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Expanding the genetic code of Pseudomonas aeruginosa

第十届全国化学生物学学术会议

作者： Huangtao Zheng Shixian Lin Peng R Chen Beijing National Laboratory for Molecular Sciences College of Chemistry and Molecular EngineeringPeking University

The genetic code expansion strategy, which incorporates unnatural amino acids with diverse functionalities into specific sites of target proteins, has been proved to facilitate biological study in many organisms. Here we have extended the pyrrolysine-based genetic code expansion strategy in Pseudomonas aeruginosa（PA）, a common opportunistic human pathogen. Using this system, a photo-crosslinking amino acid was incorporated into type III secretion effector ExoS, which allowed the identification of its interaction proteins. Additionally, an azide-bearing amino acid was introduced into PA flagellin, FliC. which allowed in vivo labeling and imaging of PA flagella. This work will provide powerful tools for a wide range of studies on Pseudomonas aeruginosa.

关键词： genetic code expansion Unnatural amino acids Pseudomonas aeruginosa Bacterial pathogen

Simplified methodology for a modular and genetically expanded protein synthesis in cell-free systems

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Synthetic and Systems Biotechnology 2019年第4期4卷 189-196页

作者： Yonatan Chemla Eden Ozer Michael Shaferman Ben Zaad Rambabu Dandela Lital Alfonta Department of Life Sciences and Ilse Katz Institute for Nanoscale Science and Technology Ben-Gurion University of the NegevP.O.Box.653Beer-Sheva8410501Israel Institute of Chemical Technology-Indian Oil Odisha campusIIT Kharagpur extension centerMouza SamantpuriBhubaneswar751013OdishaIndia

genetic code expansion,which enables the site-specific incorporation of unnatural amino acids into proteins,has emerged as a new and powerful tool for protein ***,it is mainly utilized inside living cells for a myriad of ***,the utilization of this technology in a cell-free,reconstituted platform has several advantages over living *** typical limitations to the employment of these systems are the laborious and complex nature of its preparation and ***,we describe a simplified method for the preparation of this system from Escherichia coli cells,which is specifically adapted for the expression of the components needed for cell-free genetic code ***,we propose and demonstrate a modular approach to its *** this approach,it is possible to prepare and store different extracts,harboring various translational components,and mix and match them as needed for more than four years retaining its high *** demonstrate this with the simultaneous incorporation of two different unnatural amino acids into a reporter ***,we demonstrate the advantage of cell-free systems over living cells for the incorporation ofδ-thio-boc-lysine into ubiquitin by using the methanosarcina mazei wild-type pyrrolysyl tRNACUA and tRNA-synthetase pair,which could not be achieved in a living cell.

关键词： Cell free system genetic code expansion Thio-lysine Simplified extract preparation

Light-controlled phosphorylation in the TrkA-Y785 site by photosensitive UAAs activates the MAPK/ERK signaling pathway

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BIOCELL 2023年第6期47卷 1377-1388页

作者： SHU ZHAO SHIXIN YE School of Life Sciences Nantong UniversityNantong226019China Institute National de la Sante et de la Recherche Medicale(INSERM)U1195 Bicetre HospitalParis-Saclay UniversityLe Kremlin-Bicêtre94276France

Background:This paper aims to establish a light-controlled phosphorylation detection method at the Y785 site of tropomyosin receptor kinase A(TrkA)receptor in mammalian cells by using genetic code expansion technology and detecting the effects of optical activation of this site on the downstream MAPK/ERK *** study is based on the current situation that the regulatory mechanism of TrkA phosphorylation has not been fully ***:Two photosensitive unnatural amino acids,p-azido-L-phenylalanine(AzF)and photo-caged tyrosine(ONB)were introduced into the TrkA-Y785 site by genetic code expansion technology and site-directed *** blotting and laser confocal imaging were conducted to analyze the effects of this site on activating the MAPK/ERK pathway and nerve cell differentiation before and after ***:Our results supplemented the light-controlled results of the TrkA-Y785 site based on our previous research and verified that Y785 also makes important contributions in regulating the MAPK/ERK ***:This study demonstrated the significant contributions of the TrkAY785 site in regulating the ERK pathway by precisely controlling the phosphorylation state of a single tyrosine site.

关键词： Tropomyosin receptor kinase A genetic code expansion Y785 P-azido-L-phenylalanine Photo-caged tyrosine