在vivo中对多位蛋白残留物进行基因编码
Jun Liu1, Shanshan Li1,2, Nayyar A Aslam3
1Department of Pharmaceutical Chemistry and the Cardiovascular Research Institute , University of California San Francisco , 555 Mission Bay Boulevard South , San Francisco , California 94158 , United States.
Journal of the American Chemical Society
|June 12, 2019
概括
研究人员开发了一种新的非自然氨基酸 (FnbY),在光激活时在蛋白质中形成共价键. 这种方法针对9种天然氨基酸残留物,扩大了蛋白质工程和生物治疗的可能性.
科学领域:
- 生物化学
- 分子生物学
- 蛋白质工程
背景情况:
- 基因编码的非自然氨基酸 (UAAs) 能够在体内进行蛋白质修饰.
- 目前的UAAs具有有限的残留特异性,限制了应用.
研究的目的:
- 通过基因编码一种新的Uaa,FnbY,用于体内蛋白质的共价修饰.
- 扩大UAAS所针对的天然氨基酸残留物范围.
主要方法:
- 在大肠杆菌和哺乳动物细胞中FnbY的遗传编码.
- 对FnbY进行光激活以产生反应性甲基 (QM).
- 对蛋白质中的各种天然氨基酸残留物的QM反应性的分析.
主要成果:
- 在活细胞中成功编码和光激活FnbY.
- 光激活的FnbY准了九种自然残留物:Cys,Lys,His,Tyr,Trp,Met,Arg,Asn和Gln.
- 与现有方法相比,FnbY的交叉连接效率更高,中间产品寿命更长.
结论:
- 通过FnbY显著扩大了对体内共价蛋白向的残留物.
- 在化学生物学,生物治疗和蛋白质工程中,FnbY的可光激活,多目标性质具有广泛的用途.
相关概念视频
Covalently Linked Protein Regulators
8.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
8.8K
Covalently Linked Protein Regulators
2.0K
2.0K
Covalent Bonds
160.6K
Overview
160.6K
Covalent Bonds
10.1K
Overview
When two atoms share electrons to complete their valence shells, they create a covalent bond. An atom's electronegativity—the force with which shared electrons are pulled towards an atom—determines how the electrons are shared. Molecules formed with covalent bonds can be either polar or nonpolar. Atoms with similar electronegativities form nonpolar covalent bonds; the electrons are shared equally. Atoms with different electronegativities share electrons unequally,...
When two atoms share electrons to complete their valence shells, they create a covalent bond. An atom's electronegativity—the force with which shared electrons are pulled towards an atom—determines how the electrons are shared. Molecules formed with covalent bonds can be either polar or nonpolar. Atoms with similar electronegativities form nonpolar covalent bonds; the electrons are shared equally. Atoms with different electronegativities share electrons unequally,...
10.1K
Network Covalent Solids
16.1K
Network covalent solids contain a three-dimensional network of covalently bonded atoms as found in the crystal structures of nonmetals like diamond, graphite, silicon, and some covalent compounds, such as silicon dioxide (sand) and silicon carbide (carborundum, the abrasive on sandpaper). Many minerals have networks of covalent bonds.
To break or to melt a covalent network solid, covalent bonds must be broken. Because covalent bonds are relatively strong, covalent network solids are typically...
To break or to melt a covalent network solid, covalent bonds must be broken. Because covalent bonds are relatively strong, covalent network solids are typically...
16.1K
Oxidation of Phenols to Quinones
4.6K
In the presence of oxidizing agents, phenols are oxidized to quinones. Quinones can be easily reduced back to phenols using mild reducing agents. The electron-donating hydroxyl group enhances the reactivity of the aromatic ring, enabling oxidation of the ring even in the absence of an α hydrogen.
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox...
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox...
4.6K


